Vincent Massey
Bibliography
Massey 1
Vincent Massey—Bibliography
(1)
1949
(2)
1950
(3)
1950
(4)
1950
(5)
1951
(6)
(7)
(8)
1951
1952
1953
(9)
(10)
1953
1953
(11)
1954
(12)
1954
(13)
1954
(14)
1956
(15)
1956
(16)
1956
(17)
1956
(18)
1956
(19)
1957
(20)
1957
(21)
1957
(22)
1957
(23)
1957
(24)
1957
(25)
1958
(26)
1958
(27)
1959
(28)
(29)
1959
1960
(30)
1960
(31)
1960
(32)
1960
Massey, V., Rogers, W. P. The Tricarboxylic Acid Cycle in Nematode Parasites. Nature 163, 9099l0.
Massey, V., and Rogers, W. P. The Intermediary Metabolism of Nematode Parasites. I. General
Reactions of the Tricarboxylic Acid Cycle. Aust. J. Sci. Res. B3, 251-264.
Massey, V., and Rogers, W. P. Fluoroacetic and the Tricarboxylic Acid Cycle in Nematode Parasites.
Nature 165, 681-682.
Massey, V., and Rogers, W. P. Effects of Oxygen Carriers and Oxygen Tensions on Fluoroacetate
Inhibition of Citrate Utilization. Nature 166, 951-952.
Massey, V., and Rogers, W. P. Conditions Affecting the Action of Fluoroacetate on the Metabolism
of Nematode Parasites and Vertebrate Animals. Aust. J. Sci. Res. B4, 561-574.
Massey, V. Crystallization of Fumarase. Nature 167, 769-771.
Massey, V. The Crystallization of Fumarase. Biochem. J. 51, 490-494.
Massey, V. Studies on Fumarase. II. The Effect of Inorganic Anions on Fumarase Activity. Biochem.
J. 53, 67-71.
Massey, V. Studies on Fumarase. III. The Effect of Temperature. Biochem. J. 53, 72-79.
Massey, V. Studies on Fumarase. IV. The Effect of Inhibitors on Fumarase Activity. Biochem. J. 55,
172-177.
Alberty, R. A., and Massey, V. On the Interpretation of the pH Variation of the Maximum Initial
Velocity of an Enzyme-Catalyzed Reaction. Biochim. Biophys. Acta 13, 347-353.
Massey, V., and Alberty, R. A. Ionization Constants of Fumarase. Biochim. Biophys Acta 13, 354359.
Alberty, R. A., Massey, V., Frieden, C., and Fuhlbrigge, A. R. Studies of the Enzyme Fumarase. III.
The Dependence of the Kinetic Constants at 25° upon the Concentration and pH of Phosphate
Buffers. J. Amer. Chem. Soc. 76, 2485-2493.
Hartley, B. S., and Massey, V. The Active Centre of Chymotrypsin. I. Labelling with a Fluorescent
Dye. Biochim. Biophys. Acta 21, 58-70.
Massey, V., and Hartley, B. S. The Active Centre of Chymotrypsin. II. Reaction with
Fluorodinitrobenzene. Biochim. Biophys. Acta 21, 361-367.
Singer, T. P., Kearney, E. B., and Massey, V. Observation on the Flavin Moiety of Succinic
Dehydrogenase. Arch. Biochem. Biophys. 60, 255-257.
Singer, T. P., Massey, V., and Kearney, E. B. On the Reversibility of Succinic Dehydrogenase.
Biochim. Biophys. Acta 19, 200-201.
Singer, T. P., Thimot, N. Z., Massey, V., and Kearney, E. B. Purification and Properties of Succinic
Dehydrogenase from Yeast. Arch. Biochem. Biophys. 62, 497-499.
Singer, T. P., Massey, V., and Kearney, E. B. Studies on Succinic Dehydrogenase. V. Isolation and
Properties of the Dehydrogenase from Baker's Yeast. Arch. Biochem. Biophys. 69, 405-421.
Johnson, P., and Massey, V. Sedimentation Studies on Fumarase. Biochim. Biophys. Acta 23, 544550.
Massey, V., and Singer, T. P. Studies on Succinic Dehydrogenase. III. The Fumaric Reductase
Activity of Succinic Dehydrogenase. J. Biol. Chem. 263-274.
Massey, V., and Singer, T. P. Studies on Succinic Dehydrogenase. VI. The Reactivity of Beef Heart
Succinic Dehydrogenase with Electron Carriers. J. Biol. Chem. 229, 755-762.
Massey, V. Studies on Succinic Dehydrogenase. VII. Valency State of the Iron in Beef Heart Succinic
Dehydrogenase. J. Biol. Chem. 229, 763-770.
Singer, T. P., and Massey, V. Experimental Foundations of the Concept of Metal-Flavoprotein
Catalysis. Rec. Chem. Prog. 18, 201-244.
Massey, V. The Identity of Diaphorase and Lipoic Dehydrogenase. Biochim. Biophys. Acta 30, 205206.
Massey, V. The Role of Iron in Beef Heart Succinic Dehydrogenase. Biochim. Biophys. Acta 30,
500-509.
Massey, V. The Microestimation of Succinate and the Extinction Coefficient of Cytochrome c.
Biochim. Biophys. Acta 34, 255-256.
Massey, V. The Role of Diaphorase in Ketoglutarate Oxidation. Biochim. Biophys. Acta 32, 286-287.
Veeger, C., and Massey, V. Inhibition of Lipoyl Dehydrogenase by Trace Metals. Biochim. Biophys.
Acta 37, 181-183.
Massey, V. The Relation of Diaphorase and Cytochrome Reductase. Biochim. Biophys. Acta 37, 310314.
Massey, V. The Identity of Diaphorase and Lipoyl Dehydrogenase. Biochim. Biophys. Acta 37, 314322.
Massey, V. The Composition of the Ketoglutarate Dehydrogenase Complex. Biochim. Biophys. Acta
38, 447-460.
Massey 2
(33)
1960
(34)
1960
(35)
1961
(36)
1961
(37)
1962
(38)
1962
(39)
1962
(40)
1962
(41)
1962
(42)
1962
(43)
1963
(44)
1963
(45)
1963
(46)
1964
(47)
1964
(48)
1965
(49)
1965
(50)
1965
(51)
1965
(52)
1965
(53)
1965
(54)
1965
(55)
1966
(56)
1966
(57)
1966
(58)
1966
(59)
1966
(60)
1966
(61)
1966
(62)
1966
(63)
1967
Massey, V., Gibson, Q. H., and Veeger, C. Intermediates in the Catalytic Action of Lipoyl
Dehydrogenase. Biochim. J. 77, 341-351.
Massey, V. Substrate-Induced Denaturation of Lipoyl Dehydrogenase in Urea. J. Biol. Chem. 235, PC
47-48.
Massey, V., Palmer, G., and Bennett, R. The Purification and Some Properties of D-Amino Acid
Oxidase. Biochim. Biophys. Acta 48, 1-9.
Massey, V., and Veeger, C. Studies on the Reaction Mechanism of Lipoyl Dehydrogenase. Biochim.
Biophys. Acta 48, 33-47.
Palmer, G., and Massey, V. On the Sulphydryl Groups of Lipoamide Dehydrogenase. Biochim.
Biophys. Acta. 58, 349-350.
Veeger, C., and Massey, V. The Reaction Mechanism of Lipoamide Dehydrogenase. II. Modification
by Trace Metals. Biochim. Biophys. Acta. 64. 83-100.
Massey, V., and Palmer, G. Charge Transfer Complexes of Lipoyl Dehydrogenase and Free Flavins.
J. Biol. Chem. 237, 2347-2358.
Gibson, Q. H., Massey, V., and Atherton, N. M. The Nature of Compounds Present in Mixtures of
Oxidized and Reduced Flavin Mononucleotides. Biochem. J. 85, 369-383.
Massey, V., and Atherton, N. M. On the Reaction between Dihydrolipoic Acid and Flavins: Spectral
Changes Induced by Flavin-Peroxide Interaction. J. Biol. Chem. 237, 2965-2967.
Massey, V., Hofmann, T., and Palmer, G. The Relation of Function and Structure in Lipoyl
Dehydrogenase. J. Biol. Chem. 237, 3820-3828.
Deal, W. C., Rutter, W. J., Massey, V., and Van Holde, K. E. Reversible Alteration of the Structure of
Enzymes in Acidic Solution. Biochem. Biophys. Res. Commun. 10, 49-54.
Massey, V., and Swoboda, B. E. P. The Flavin Composition of Pig Heart Muscle Preparations.
Biochem. Zeit. 338, 474-484.
Veeger, C., and Massey, V. A New NAD+-Dependent Spectral Species of Lipoamide
Dehydrogenase. Biochim. Biophys. Acta 67, 679-681.
Massey, V., and Gibson, Q. H. The Role of Semiquinones in Flavoprotein Catalysis. Fed. Proc. 23,
18-29.
Gibson, Q. H., Swoboda, B. E. P., and Massey, V. Kinetics and Mechanism of Action of Glucose
Oxidase. J. Biol. Chem. 239, 3927-3934.
Wren, A., and Massey, V. Lipoyl Dehydrogenase from Saccharomyces cerevisiae. I. Purification and
Some Properties. Biochim. Biophys. Acta 110, 329-336.
Miller, R. W., and Massey, V. Dihydroorotic Dehydrogenase. I. Some Properties of the Enzyme. J.
Biol. Chem. 240, 1453-1465.
Miller, R. W., and Massey, V. Dihydroorotic Dehydrogenase. II. Oxidation and Reduction of
Cytochrome c. J. Biol. Chem. 240, 1466-1472.
Swoboda, B. E. P., and Massey, V. Purification and Properties of the Glucose Oxidase from
Aspergillus niger. J. Biol. Chem. 240, 2209-2215.
Brumby, P. E., Miller, R. W., and Massey, V. The Content and Possible Catalytic Significance of
Labile Sulfide in Some Metalloflavoproteins. J. Biol. Chem. 240, 2222-2228.
Massey, V., and Ganther, H. On the Interpretation of the Absorption Spectra of Flavoproteins, with
Special Reference to D-Amino Acid Oxidase. Biochemistry 4, 1161-1173.
Massey, V., and Williams, C. H., Jr. On the Reaction Mechanism of Yeast Glutathione Reductase. J.
Biol. Chem. 240, 4470-4480.
Wren, A., and Massey, V. Lipoyl Dehydrogenase from Saccharomyces cerevisiae. II. Kinetic and
Inhibitor Studies. Biochim. Biophys. Acta 122, 436-449.
Massey, V., Curti, B., and Ganther, H. A Temperature-Dependent Conformational Change in DAmino Acid Oxidase and its Effect on Catalysis. J. Biol. Chem. 241, 2347-2357.
Antonini, E. M., Brunori, M., Bruzzesi, M. R., Chiancone, E., and Massey, V. AssociationDissociation Phenomena of D-Amino Acid Oxidase. J. Biol. Chem. 241, 2358-2366.
Swoboda, B. E. P., and Massey, V. On the Reaction of the Glucose Oxidase from Aspergillus niger
with Bisulfite. J. Biol. Chem. 241, 3409-34l6.
Massey, V., and Curti, B. A New Method of Preparation of D-Amino Acid Oxidase Apoprotein and a
Conformational Change after its Combination with Flavin Adenine Dinucleotide. J. Biol. Chem. 241,
3417-3423.
Casola, L., Brumby, P. E., and Massey, V. The Reversible Conversion of Lipoyl Dehydrogenase to an
Artifactual Enzyme by Oxidation of Sulfhydryl Groups. J. Biol. Chem. 241, 4977-4984.
Casola, L., and Massey, V. Differential Effects of Mercurial on the Lipoyl Reductase and Diaphorase
Activities of Lipoyl Dehydrogenase. J. Biol. Chem. 241, 4985-4993.
Massey, V., and Palmer, G. On the Existence of Spectrally Distinct Classes of Flavoprotein
Semiquinones. A New Method for the Quantitative Production of Flavoprotein Semiquinones.
Biochemistry 5, 3181-3189.
Hemmerich, P., Massey, V. and Weber, G. Photo-Induced Benzyl Substitution of Flavins by
Phenylacetate: A Possible Model for Flavoprotein Catalysis. Nature 213, 728-730.
Massey 3
(64)
1967
(65)
1967
(66)
1968
(67)
1968
(68)
1968
(69)
1968
(70)
1969
(71)
1969
(72)
1969
(73)
1969
(74)
1969
(75)
1969
(76)
1969
(77)
1969
(78)
1969
(79)
1969
(80)
1969
(81)
1969
(82)
1969
(83)
1969
(84)
1970
(85)
1970
(86)
1970
(87)
1970
(88)
1970
(89)
1971
(90)
1971
Massey, V., and Curti, B. On the Reaction Mechanism of Crotalus adamanteus L-Amino Acid
Oxidase. J. Biol. Chem. 242, 1259-1264.
Walker, W. H., Hemmerich, P., and Massey, V. Reduktive Photoalkylierung des Flavinkerns and
Flavinkatalysierte Photodecarboxylierung von Phenylacetat. Helv. Chim. Acta 50, 2269-2279.
Woodfin, B. M., and Massey, V. Spectrophotometric Determination of the Dissociation Constant of
Ribonuclease S'. J. Biol. Chem. 243, 889-892.
Massey, V., Curti, B., Müller, F., and Mayhew, S. G. On the Reaction of Borohydride with D- and LAmino Acid Oxidases. J. Biol. Chem. 243, 1329- 1332.
Curti, B., Massey, V., and Zmudka, M. Inactivation of Snake Venom L-Amino Acid Oxidase by
Freezing. J. Biol. Chem. 243, 2306-2314.
Zanetti, G., Williams, C. H., Jr., and Massey, V. Influence of Photo irradiation on the OxidationReduction State of Thioredoxin Reductase. J. Biol. Chem. 243, 4013-4019.
Mayhew, S. G., and Massey, V. Purification and Characterization of Flavodoxin from
Peptostreptococcus elsdenii. J. Biol. Chem. 244, 794-802.
Mayhew, S. G., Foust, G. P., and Massey, V. Oxidation-Reduction Properties of Flavodoxin from
Peptostreptococcus elsdenii. J. Biol. Chem. 244, 803-810.
Foust, G. P., Mayhew, S. G., and Massey, V. Complex Formation between Ferredoxin
Triphosphopyridine Nucleotide Reductase and Electron Transfer Proteins. J. Biol. Chem. 244, 964970.
Foust, G. P., Burleigh, B. D., Jr., Mayhew, S. G., Williams, C. H., Jr., and Massey, V. An Anaerobic
Titration Assembly for Spectrophotometric Use. Anal. Biochem. 27, 530-535.
Massey, V., Brumby, P. E., Komai, H., and Palmer, G. Studies on Milk Xanthine Oxidase. Some
Spectral and Kinetic Properties. J. Biol. Chem. 244, 1682-1691.
Matthews, R. G., and Massey, V. Isolation of Old Yellow Enzyme in Free and Complexed Forms. J.
Biol. Chem. 244, 1779-1786.
Komai, H., Massey, V., and Palmer, G. The Preparation and Properties of Deflavo Xanthine Oxidase.
J. Biol. Chem. 244, 1692-1700.
Palmer, G., and Massey, V. Electron Paramagnetic Resonance and Circular Dichroism Studies on
Milk Xanthine Oxidase. J. Biol. Chem. 244, 2614-2620.
Massey, V., Müller, F., Feldberg, R., Schuman, M., Sullivan, P. A., Howell, L. G., Mayhew, S. G.,
Matthews, R. G., and Foust, G. P. The Reactivity of Flavoproteins with Sulfite; Possible Relevance to
the Problem of Oxygen Reactivity. J. Biol. Chem. 244, 3999-4006.
Müller, F., and Massey, V. Flavin-Sulfite Complexes and their Structures. J. Biol. Chem. 244, 40074016.
Müller, F., Massey, V., Heizmann, C., Hemmerich, P., Lhoste, J.-M., and Gould, D. C. The Reduction
of Flavins by Borohydride: 3,4-Dihydroflavin. Structure, Absorption and Luminescence. Eur. J.
Biochem. 9, 392-401.
Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman,
M., and Sullivan, P. A. The Production of Superoxide Anion Radicals in the Reaction of Reduced
Flavins and Flavoproteins with Molecular Oxygen. Biochim. Biophys. Res. Commun. 36, 891- 897.
Ballou, D., Palmer, G., and Massey, V. Direct Demonstration of Superoxide Anion Production during
the Oxidation of Reduced Flavin and of its Catalytic Decomposition by Erythrocuprein. Biochem.
Biophys. Res. Commun. 36, 898-904.
Ludwig, M. L., Andersen, R. D., Mayhew, S. G., and Massey, V. The Structure of a Clostridial
Flavodoxin. I. Crystallographic Characterization of the Oxidized and Semiquinone Forms. J. Biol.
Chem. 244. 6047-6048.
Walker, W. H., Hemmerich, P., and Massey, V. Light-Induced Alkylation and Dealkylation of the
Flavin Nucleus. Stable Dihydroflavins: Spectral Course and Mechanism of Formation. Eur. J.
Biochem. 13, 258-266.
Massey, V., Komai, H., Palmer, G., and Elion, G. B. On the Mechanism of Inactivation of Xanthine
Oxidase by Allopurinol and Other Pyrazolo[3,4-d]- Pyrimidines. J. Biol. Chem. 245, 2837-2844.
Müller, F., Hemmerich, P., Ehrenberg, A., Palmer, G., and Massey, V. The Chemical and Electronic
Structure of the Neutral Flavin Radical as Revealed by Electron Spin Resonance Spectroscopy of
Chemically and Isotopically Substituted Derivatives. Eur. J. Biochem. 14, 185-196.
Howell, L. G., and Massey, V. A Non-Substrate Effector of p-Hydroxybenzoate Hydroxylase.
Biochem. Biophys. Res. Commun. 40, 887-893.
Massey, V., and Edmondson, D. On the Mechanism of Inactivation of Xanthine Oxidase by Cyanide.
J. Biol. Chem. 245, 6595-6598.
Zimmerman, S. E., Brown, R. K., Curti, B., and Massey, V. Immunochemical Studies of L-Amino
Acid Oxidase. Biochim. Biophys. Acta 229, 260-270.
Massey, V., Williams, C. H., Jr., and Palmer, G. The Presence of S°-Containing Impurities in
Commercial Samples of Oxidized Glutathione and their Catalytic Effect on the Reduction of
Cytochrome c. Biochem. Biophys. Res. Commun. 42, 730-738.
Massey 4
(91)
1971
(92)
1971
(93)
1972
(94)
1971
(95)
1971
(96)
1971
(97)
1971
(98)
1971
(99)
1971
(100)
1972
(101)
1972
(102)
1972
(103)
1972
(104)
1972
(105)
1972
(106)
1972
(107)
1972
(108)
1973
(109)
1973
(110)
1973
(111)
1973
(112)
1973
(113)
1973
(114)
1973
(115)
1973
(116)
1974
(117)
1974
(118)
1974
(119)
1974
Schuman, M., and Massey, V. Purification and Characterization of Glycolic Acid Oxidase from Pig
Liver. Biochim. Biophys. Acta 227, 500-520.
Schuman, M., and Massey, V. Effect of Anions on the Catalytic Activity of Pig Liver Glycolic Acid
Oxidase. Biochim. Biophys. Acta 227, 521-537.
Mayhew, S. G., and Massey, V. Evidence for a Novel Flavin Prosthetic Group Associated with
NADH Dehydrogenase from Peptostreptococcus elsdenii. Biochim. Biophys. Acta 235, 303-310.
Brunori, M., Rotilio, G. C., Antonini, E., Curti, B., Branzoli, U., and Massey, V. Oxidation-Reduction
Potentials of D-Amino Acid Oxidase. J. Biol. Chem. 246, 3140-3144.
Tanaka, M., Haniu, M., Matsueda, G., Yasunobu, K., Mayhew, S., and Massey, V. Amino Acid
Sequence of the Peptostreptococcus elsdenii Flavodoxin. Biochem. Biophys. Res. Commun. 44, 886892.
Tanaka, M., Haniu, M., Matsueda, G., Yasunobu, T., Mayhew, S. G., and Massey, V. Amino- and
Carboxyl-Terminal Amino Acid Sequences of the Peptostreptococcus elsdenii and Clostridium
pasteurianum Flavodoxins. Biochemistry 10, 3041-3046.
Spector, T., and Massey, V. Interactions of Substrate and Non-Substrate Effectors with pHydroxybenzoate Hydroxylase from Pseudomonas fluorescens. Biochem. Biophys. Res. Commun. 45,
1219-1226.
Engel, P. C., and Massey, V. The Purification and Properties of Butyryl- Coenzyme A
Dehydrogenase from Peptostreptococcus elsdenii. Biochem. J. 125, 879-887.
Engel, P. C., and Massey, V. Green Butyryl-Coenzyme A Dehydrogenase; An Enzyme-AcylCoenzyme A Complex. Biochem. J. 125, 889-902.
Müller, F., Brustlein, M., Hemmerich, P., Massey, V., and Walker, W. H. Light-Absorption Studies
on Neutral Flavin Radicals. Biochemistry 25, 573-580.
Edmondson, D., Massey, V., Palmer, G., Beacham, L. M., III., and Elion, G. B. The Resolution of
Active and Inactive Xanthine Oxidase by Affinity Chromatography. J. Biol. Chem. 247, 1597-1604.
Howell, L. G., Spector, T., and Massey, V. Purification and Properties of p-Hydroxybenzoate
Hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247, 4340-4350.
Spector, T., and Massey, V. Studies on the Effector Specificity of p- Hydroxybenzoate Hydroxylase
from Pseudomonas fluorescens. J. Biol. Chem. 247, 4679-4687.
Spector, T., and Massey, V. p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens:
Evidence for an Oxygenated Flavin Intermediate. J. Biol. Chem. 247, 5632-5636.
Spector, T., and Massey, V. p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens.
Reactivity with Oxygen. J. Biol. Chem. 247, 7123-7127.
Walsh, C. T., Schonbrunn, A., Lockridge, O., Massey, V., and Abeles, R. H. Inactivation of a
Flavoprotein, Lactate Oxidase, by an Acetylenic Substrate. J. Biol. Chem. 247, 6004-6006.
Lockridge, O., Massey, V., and Sullivan, P. A. Mechanism of Action of the Flavoenzyme Lactate
Oxidase. J. Biol. Chem. 247, 8097-8106.
Walsh, C. T., Krodel, E., Massey, V., and Abeles, R. H. Studies on the Elimination Reaction of DAmino Acid Oxidase with -Amino--chlorobutyrate. Further Evidence for Abstraction of Substrate
a-Hydrogen as a Proton. J. Biol. Chem. 248, 1946-1955.
Strickland, S., and Massey, V. The Purification and Properties of the Flavoprotein Melilotate
Hydroxylase. J. Biol. Chem. 248, 2944-2952.
Strickland, S., and Massey, V. The Mechanism of Action of the Flavoprotein Melilotate Hydroxylase.
J. Biol. Chem. 248, 2953-2962.
Tanaka, M., Haniu, M., Yasunobu, K. T., Mayhew, S., and Massey, V. The Primary Structure of
Peptostreptococcus elsdenii Flavodoxin. J. Biol. Chem. 248, 4354-4366.
Mayhew, S. G., and Massey, V. Studies on the Kinetics and Mechanism of Reduction of Flavodoxin
from Peptostreptococcus elsdenii by Sodium Dithionite. Biochim. Biophys. Acta 315, 181-190.
Müller, F., Mayhew, S. G., and Massey, V. The Effect of Temperature on the Absorption Spectra of
Free and Protein-Bound Flavins. Biochemistry 12, 4654-4662.
Edmondson, D., Ballou, D., Van Heuvelin, A., Palmer, G., and Massey, V. Kinetic Studies on the
Substrate Reduction of Xanthine Oxidase. J. Biol. Chem. 248, 6135-6144.
Walsh, C. T., Lockridge, O., Massey, V., and Abeles, R. H. Studies on the Mechanism of Action of
the Flavoenzyme Lactate Oxidase. Oxidation and Elimination with -Chlorolactate. J. Biol. Chem.
248, 7049-7054.
Ghisla, S., Massey, V., Lhoste, J-M., and Mayhew, S. G. Fluorescence and Optical Characteristics of
Reduced Flavins and Flavoproteins. Biochemistry 13, 589-597.
Entsch, B., Massey, V., and Ballou, D. P. Intermediates in Flavoprotein Catalyzed Hydroxylations.
Biochem. Biophys. Res. Commun. 57, 1018-1025.
Flashner, M. I. S., and Massey, V. Purification and Properties of L- Lysine Monooxygenase from
Pseudomonas fluorescens. J. Biol. Chem. 249, 2579-2586.
Flashner, M. I. S., and Massey, V. Regulatory Properties of the Flavoprotein L-Lysine
Monooxygenase. J. Biol. Chem. 249, 2587-2592.
Massey 5
(120)
1974
(121)
1974
(122)
1974
(123)
1974
(124)
1974
(125)
1975
(126)
1975
(127)
1975
(128)
1975
(129)
1976
(130)
1976
(131)
1976
(132)
1976
(133)
1976
(134)
1976
(135)
1976
(136)
1977
(137)
1977
(138)
1977
(139)
1977
(140)
1977
(141)
1978
(142)
1978
(143)
1978
(144)
1978
(145)
1979
(146)
1979
(147)
1979
(148)
1979
Massey, V., and Ghisla, S. Role of Charge Transfer Interactions in Flavoprotein Catalysis. Ann. N. Y.
Acad. Sci. 227, 446-465.
Branzoli, U., and Massey, V. Preparation of Aldehyde Oxidase in its Native and Deflavo Forms. J.
Biol. Chem. 249, 4339-4345.
Branzoli, U., and Massey, V. Evidence for an Active Site Persulfide Residue in Rabbit Liver
Aldehyde Oxidase. J. Biol. Chem. 249, 4346-4349.
Olson, J. S., Ballou, D. P., Palmer, G., and Massey, V. The Reaction of Xanthine Oxidase with
Molecular Oxygen. J. Biol. Chem. 249, 4350-4362.
Olson, J. S., Ballou, D. P., Palmer, G., and Massey, V. The Mechanism of Action of Xanthine
Oxidase. J. Biol. Chem. 249, 4363-4382.
Ghisla, S., and Massey, V. Mechanism of Inactivation of the Flavoenzyme Lactate Oxidase by
Oxalate. J. Biol. Chem. 250, 577-584.
Strickland, S., Schopfer, L. M., and Massey, V. Kinetic and Mechanistic Studies on the Reaction of
Melilotate Hydroxylase with Deuterated Melilotate. Biochemistry 14, 2230-2235.
Strickland, S., Palmer, G., and Massey, V. Determination of Dissociation Constants and Specific Rate
Constants of Enzyme-Substrate (or Protein- Ligand) Interactions from Rapid Reaction Kinetic Data.
J. Biol. Chem. 250, 4048-4052.
Matthews, R. G., Massey, V., and Sweeley, C. C. Identification of p- Hydroxybenz-aldehyde as the
Ligand in the Green Form of Old Yellow Enzyme. J. Biol. Chem. 250, 9294-9298.
Entsch, B., Ballou, D. P., and Massey, V. Flavin-Oxygen Derivatives Involved in Hydroxylation by
p-Hydroxybenzoate Hydroxylase. J. Biol. Chem. 251, 2550-2563.
Ghisla, S., Ogata, H., Massey, V., Schonbrunn, A., Abeles, R. H., and Walsh, C. T. Kinetic Studies on
the Inactivation of L-Lactate Oxidase by the Acetylenic Suicide Substrate 2-Hydroxy-3-butynoate.
Biochemistry 15, 1791-1797.
Schonbrunn, A., Abeles, R. H., Walsh, C. T., Ghisla, S., Ogata, H., and Massey, V. The Structure of
the Covalent Flavin Adduct Formed between L- Lactate Oxidase and the Suicide Substrate 2Hydroxy-3-butynoate. Biochemistry 15, 1798-1807.
Abramovitz, A. S., and Massey, V. Purification of Intact Old Yellow Enzyme using an Affinity
Matrix for the Sole Chromatographic Step. J. Biol. Chem. 251, 5321-5326.
Abramovitz, A. S., and Massey. Interaction of Phenols with Old Yellow Enzyme. Physical Evidence
for Charge-Transfer Complexes. J. Biol. Chem. 251, 5327-5336.
Stankovich, M. T., and Massey, V. Determination of the Redox Potential of Deazariboflavin by
Equilibration with Flavins. Biochim. Biophys. Acta 452, 335-344.
Entsch, B., Ballou, D.P., Husain, M., and Massey, V. Catalytic Mechanism of p-Hydroxybenzoate
Hydroxylase with p-Mercaptobenzoate as Substrate. J. Biol. Chem. 251, 7367-7379.
Ghisla, S., Entsch, B., Massey, V., and Husain, M. On the Structure of Flavin-Oxygen Intermediates
Involved in Enzymatic Reactions. Eur. J. Biochem. 76. 139-148.
Quay, S., and Massey, V. Effect of pH on the Interaction of Benzoate and D-Amino Acid Oxidase.
Biochemistry, 16, 3348-3354.
Massey, V., and Hemmerich, P. A Photochemical Procedure for Reduction of Oxidation-Reduction
Proteins Employing Deazariboflavin as Catalyst. J. Biol. Chem. 252, 5612-5614.
Ghisla, S., and Massey, V. Studies on the Mechanism of Action of the Flavoenzyme Lactate Oxidase.
J. Biol. Chem. 252, 6729-6735.
Hemmerich, P., Massey, V., and Fenner, H. Flavin and 5-Deazaflavin: A Chemical Evaluation of
"modified" Flavoproteins with Respect to the Mechanisms of Redox Biocatalysis. FEBS Lett. 84, 521.
Massey, V., Stankovich, M., and Hemmerich, P. Light-Mediated Reduction of Flavoproteins with
Flavins as Catalysts. Biochemistry 17, 1-8.
Massey, V., and Hemmerich, P. Photoreduction of Flavoproteins and Other Biological Compounds
Catalyzed by Deazaflavins. Biochemistry 17, 9-17.
Stankovich, M., Schopfer, L., Massey, V. Determination of Glucose Oxidase Oxidation-Reduction
Potentials and the Oxygen Reactivity of Fully Reduced and Semiquinoid Forms. J. Biol. Chem. 253,
4971-4979.
Moore, E., Cardemil, E., and Massey, V. Production of a Covalent Flavin Linkage in Lipoamide
Dehydrogenase. Reaction with 8-Cl-FAD. J. Biol. Chem. 253, 6413-6422.
Fenner, H., Grauert, R., Hemmerich, P., Michel, H., and Massey, V. 5- Thia-5-Deazaflavin, a le-Transferring Flavin Analog. Eur. J. Biochem. 95, 183-191.
Massey, V., and Mendelsohn, L. D. Immobilized Glucose Oxidase and D-Amino Acid Oxidase: A
Convenient Method for Purification of Flavin Adenine Dinucleotide and Its Analogs. Analytical
Biochem. 95, 156-159.
Husain, M., and Massey, V. Kinetic Studies on the Reaction of p-Hydroxybenzoate Hydroxylase.
Agreement of Steady State and Rapid Reaction Data. J. Biol. Chem. 254, 6657-6666.
Moore, E. G., Ghisla, S., and Massey, V. Properties of Flavins Where the 8-Methyl Group is
Replaced by Mercapto-Residues. J. Biol. Chem. 254, 8173-8178.
Massey 6
(149)
1979
(150)
1979
(151)
1979
(152)
1979
(153)
1979
(154)
1979
(155)
1979
(156)
1980
(157)
1980
(158)
1980
(159)
1980
(160)
1980
(161)
1980
(162)
1980
(163)
1980
(164)
1980
(165)
1980
(166)
1980
(167)
1980
(168)
1981
(169)
1981
(170)
1981
(171)
1981
(172)
1981
(173)
(174)
1981
1982
(175)
1982
(176)
1982
(177)
1982
Massey, V., Ghisla, S., and Moore, E. G. 8-Mercaptoflavins as Active Site Probes of Flavoenzymes.
J. Biol. Chem. 254, 9640-9650.
Olson, S. T., and Massey, V. Purification and Properties of the Flavoenzyme D-Lactate
Dehydrogenase from Megasphaera elsdenii. Biochemistry 18, 4714-4724.
Olson, S. T., Massey, V., Ghisla, S., and Whitfield, C. D. Suicide Inactivation of the Flavoenzye DLactate Dehydrogenase by -Hydroxybutynoate. Biochemistry 18, 4724-4732.
Ghisla, S., Olson, S. T., Massey, V., and Lhoste, J.-M. Structure of the Flavin Adduct Formed in the
Suicide Reaction of -Hyroxybutynoate with D-Lactate Dehydrogenase. Biochemistry 18, 47334742.
Schopfer, L. M., and Massey, V. Kinetic and Mechanistic Studies on the Reduction of Melilotate
Hydroxylase by Reduced Pyridine Nucleotides. J. Biol. Chem. 254, 10634-10643.
Ghisla, S., Massey, V., and Choong, Y. S. Covalent Adducts of Lactate Oxidase. Photochemical
Formation and Structure Identification. J. Biol. Chem. 254, 10662-10669.
Visser, A. J. W. G., Ghisla, S., Massey, V., Müller, F., and Veeger, C. Fluorescence Properties of
Reduced Flavins and Flavoproteins. Eur. J. Biochem. 101, 13-21.
Massey, V., Husain, M., and Hemmerich, P. Photodehalogenation of 7- and 8-Halogen-Substituted
Flavins. Photochemistry of the Reduced Flavin Chromophore. J. Biol. Chem. 255, 1393-1398.
Entsch, B., Husain, M., Ballou, D. P., Massey, V., and Walsh, C. Oxygen Reactivity of pHydroxybenzoate Hydroxylase Containing 1-Deaza-FAD. J. Biol. Chem. 255, 1420-1429.
Massey, V., Ghisla, S., and Kieschke, K. Studies on the Reaction Mechanism of Lactate Oxidase.
Formation of Two Covalent Flavin-Substrate Adducts on Reaction with Glycollate. J. Biol. Chem.
255, 2796-2806.
Nishino, T., Massey, V., and Williams, C. H., Jr. Chemical Modifications of D-Amino Acid Oxidase.
Evidence for Active Site Histidine, Tyrosine and Arginine Residues. J. Biol. Chem. 255, 3610-3616.
Husain, M., Entsch, B., Ballou, D. P., Massey, V., and Chapman, P. J. Fluoride Elimination from
Substrates in Hydroxylation Reactions Catalyzed by p-Hydroxybenzoate Hydroxylase. J. Biol. Chem.
255, 4189-4197.
Schopfer, L. M., and Massey, V. Kinetic and Mechanistic Studies on the Oxidation of the Melilotate
Hydroxylase-2-OH Cinnamate Complex by Molecular Oxygen. J. Biol. Chem. 255, 5355-5363.
Ghisla, S., and Massey, V. Studies on the Catalytic Mechanism of Lactate Oxidase. Formation of
Enantiomeric Flavin-N5-Glycollyl Adducts via Carbanion Intermediates. J. Biol. Chem. 255, 56885696.
Nishino, T., Nishino, T., and Massey, V. Effects of Nitroaromatic Compounds on Spectra of DAmino Acid Oxidase. Biochem. Biophys. Res. Commun. 95, 312-319.
Massey, V., and Hemmerich, P. Active Site Probes of Flavoproteins. Biochemical Society
Transactions 8, 246-257.
Olson, S.T., and Massey, V. Reactivity of Sulfhydryl Groups of the Flavoenzyme D-Lactate
Dehydrogenase and Effect on Catalytic Activity. Biochemistry 19, 3137-3144.
Choong, Y. S., and Massey, V. Stabilization of Lactate Oxidase Flavin Anion Radical by Complex
Formation. J. Biol. Chem. 255, 8672-8677.
Massey, V. The Biological and Chemical Versatility of Riboflavin. Univ. Mich. Med. Center J. 46,
28-37.
Vermilion, J. L., Ballou, D. P., Massey, V., and Coon, M. J. Separate Roles for FMN and FAD in
Catalysis by Liver Microsomal NADPH-Cytochrome P-450 Reductase. J. Biol. Chem. 256, 266-277.
Schopfer, L. M., Massey, V., and Claiborne, A. Active Site Probes of Flavoproteins. Determination of
the Solvent Accessibility of the Flavin Position 8 for a Series of Flavoproteins. J. Biol. Chem. 256,
7329-7337.
Choong, Y. S., and Massey, V. Studies on Lactate Oxidase Substituted with Synthetic Flavins. IsoFMN Lactate Oxidase. J. Biol. Chem. 256, 8671- 8678.
Hille, R., Fee, J. A., and Massey, V. Equilibrium Properties of Xanthine Oxidase Containing FAD
Analogs of Varying Oxidation-Reduction Potential. J. Biol. Chem. 256, 8933-8940.
Hille, R., and Massey, V. Studies on the Oxidative Half Reaction of Xanthine Oxidase. J. Biol. Chem.
256, 9090-9095.
Hille, R., and Massey, V. Tight Binding Inhibitors of Xanthine Oxidase. Pharmac. Ther. 14, 249-263.
Hemmerich, P., Massey, V., Michel, H., and Schug, C. Scope and Limitation of Single Electron
Transfer in Biology. Structure and Bonding 48, 93-123.
Claiborne, A., Massey, V., Fitzpatrick, P. F., and Schopfer, L. M. 2- Thioflavins as Active Site Probes
of Flavoproteins. J. Biol. Chem. 257, 174-182.
Fitzpatrick, P. F., and Massey, V. Thiazolidine-2-carboxylic Acid, An Adduct of Cysteamine and
Glyoxylate, as a Substrate for D-Amino Acid Oxidase. J. Biol. Chem. 257, 1166-1171.
Swenson, R. P., Williams, C. H., Jr., and Massey, V. Chemical Modification of D-Amino Acid
Oxidase. Amino Acid Sequence of the Tryptic Peptides Containing Tyrosine and Lysine Residues
Modified by Fluorodinitrobenzene. J. Biol. Chem. 257, 1937-1944.
Massey 7
(178)
1982
(179)
1982
(180)
1982
(181)
1982
(182)
1982
(183)
1982
(184)
1982
(185)
1982
(186)
1982
(187)
1982
(188)
1982
(189)
1983
(190)
1983
(191)
1983
(192)
1983
(193)
1983
(194)
1983
(195)
1983
(196)
1983
(197)
1983
(198)
1984
(199)
1984
(200)
1984
(201)
1984
(202)
1984
(203)
1984
(204)
1984
(205)
1984
Morpeth, F. F., and Massey, V. Steady-State Kinetic Studies on D-Lactate Dehydrogenase from
Megasphera elsdenii. Biochemistry 21, 1307-1312.
Morpeth, F. F., and Massey, V. Stopped-Flow Kinetic Studies on the D- Lactate Dehydrogenase from
Megasphera elsdenii. Biochemistry 21, l3l3-1317.
Morpeth, F. F., and Massey, V. Metal Binding to D-Lactate Dehydrogenase. Biochemistry 21, 13181323.
Williamson, G., Engel, P., Mizzer, J. P., Thorpe, C., and Massey, V. Evidence that the Greening
Ligand in Native Butyryl-CoA Dehydrogenase is a CoA Persulfide. J. Biol. Chem. 257, 4314-4320.
Nishino, T., Tsushima, K., Hille, R., and Massey, V. Inhibition of Milk Xanthine Oxidase by
Fluorodinitrobenzene. J. Biol. Chem. 257, 7348-7353.
Hille, R., and Massey, V. The Presence of a Reducible Disfulfide Bond in Milk Xanthine Oxidase. J.
Biol. Chem. 257, 8898-8901.
Fitzpatrick, P. F., and Massey, V. Proton Release During the Reductive Half-reaction of D-Amino
Acid Oxidase. J. Biol. Chem. 257, 9958-9962.
Swenson, R. P., Williams, C. H., Jr., Massey, V., Ronchi, S., Minchiotti, L., Galliano, M., and Curti,
B. The Primary Structure of D-Amino Acid Oxidase from Pig Kidney. I. Isolation and Sequence of
the Tryptic Peptides. J. Biol. Chem. 257, 8817-8823.
Ronchi, S., Minchiotti, L., Galliano, M., Curti, B., Swenson, R. P., Williams, C. H., Jr., and Massey,
V. The Primary Structure of D-Amino Acid Oxidase from Pig Kidney. II. Isolation and Sequence of
Overlap Peptides and the Complete Sequence. J. Biol. Chem. 257, 8824-8834.
Mather, M., Schopfer, L. M., Massey, V., and Gennis, R. B. Studies of the Flavin Adenine
Dinucleotide Binding Region in Escherichia coli Pyruvate Oxidase. J. Biol. Chem. 257, 12887-12892.
Fitzpatrick, P. F., and Massey, V. The Kinetic Mechanism of D-Amino Acid Oxidase with D-Aminobutyrate as Substrate. Effect of Enzyme Concentration on the Kinetics. J. Biol. Chem. 257,
12916-12923.
Swenson, R. P., Williams, C. H., Jr., and Massey, V. Identification of the Histidine Residue in DAmino Acid Oxidase that is Covalently Modified during Inactivation by 5Dimethylaminonaphthalene-1-sulfonyl Chloride. J. Biol. Chem. 258, 497-502.
Choong, Y. S., and Massey, V. 2-Thioriboflavin 5'-Phosphate(2-Thio-FMN) Lactate Oxidase. Eur. J.
Biochem. 131, 501-508.
Zanetti, G., Massey, V., and Curti, B. FAD Analogues as Mechanistic and "Binding-Domain" Probes
of Spinach Ferredoxin-NADP+ Reductase. Eur. J. Biochem. 132, 201-205.
Hille, R., Stewart, R. C., Fee, J. A., and Massey, V. The Interaction of Arsenite with Xanthine
Oxidase. J. Biol. Chem. 258, 4849-4856.
Claiborne, A., and Massey, V. Mechanistic Studies of p-Hydroxybenzoate Hydroxylase Reconstituted
with 2-Thio-FAD. J. Biol. Chem. 258, 4919-4925.
Biemann, M., Claiborne, A., Ghisla, S., Massey, V., and Hemmerich, P. Oxidation of 2-Thioflavins
by Peroxides. Formation of Flavin 2-S-oxides. J. Biol. Chem. 258, 5440-5448.
Claiborne, A., Hemmerich, P., Massey, V., and Lawton, R. Reaction of 2- Thio-FAD Reconstituted pHydroxybenzoate Hydroxylase with Hydrogen Peroxide. Formation of a Covalent Flavin-Protein
Linkage. J. Biol. Chem. 258, 5433-5439.
Thorpe, C., and Massey, V. Flavin Analogue Studies of Pig Kidney General Acyl-CoA
Dehydrogenase. Biochemistry 22, 2972-2978.
Fitzpatrick, P. F., and Massey, V. The Reaction of 8-Mercaptoflavins and Flavoproteins with Sulfite.
Evidence for the Role of an Active Site Arginine in D-Amino Acid Oxidase. J. Biol. Chem. 258,
9700-9705.
Detmer, K., Schopfer, L. M., and Massey, V. Reactions of 1-Deaza-FAD-substituted Phenol
Hydroxylase and Melilotate Hydroxylase. J. Biol. Chem. 259, 1532-1538.
Swenson, R. P., Williams, C. H., Jr., and Massey, V. Methylation of the Active Center Histidine 217
in D-Amino Acid Oxidase by Methyl-p-nitrobenzenesulfonate. J. Biol. Chem. 259, 5585-5590.
Ghisla, S., Thorpe, C., and Massey, V. Mechanistic Studies with General Acyl-CoA Dehydrogenase
and Butyryl-CoA Dehydrogenase: Evidence for the Transfer of the b-Hydrogen to the Flavin N(5)Position as a Hydride. Biochemistry 23, 3154-3161.
Massey, V., Claiborne, A., Biemann, M., and Ghisla, S. 4-Thioflavins as Active Site Probes of
Flavoproteins. J. Biol. Chem. 259, 9667-9678.
Wessiak, A., Schopfer, L. M., Yuan, L., Bruice, T. C., and Massey, V. Use of Riboflavin-binding
Protein to Investigate Steric and Electronic Relationships in Flavin Analogs and Models. Proc. Natl.
Acad. Sci. U.S.A. 81, 4246-4249.
Detmer, K., and Massey, V. Effect of Monovalent Anions on the Mechanism of Phenol Hydroxylase.
J. Biol. Chem. 259, 11265-11272.
Wessiak, A., Schopfer, L. M., and Massey, V. pH Dependence of the Reoxidation of pHydroxybenzoate Hydroxylase-2,4-Dihydroxybenzoate Complex. J. Biol. Chem. 259, 12547-12556.
Biemann, M., Claiborne, A., Ghisla, S., and Massey, V. 4-Thioflavins as Active Site Probes of
Flavoproteins. Reactions with Sulfite. J. Biol. Chem. 259, 13355-13362.
Massey 8
(206)
1984
(207)
1985
(208)
1985
(209)
1985
(210)
1985
(211)
1985
(212)
1986
(213)
1986
(214)
1986
(215)
1986
(216)
1986
(217)
1986
(218)
1986
(219)
1986
(220)
1986
(221)
1986
(222)
1986
(223)
1987
(224)
1987
(225)
1987
(226)
1987
(227)
1987
(228)
1988
(229)
1988
(230)
1988
(231)
1988
(232)
1989
(233)
1989
Stewart, R.C., Hille, R. and Massey V. Characterization of Arsenite-Complexed Xanthine Oxidase at
Room Temperature. J. Biol. Chem. 259, 14426- 14436.
Detmer, K. and Massey, V. Effect of Substrate and pH on the Oxidative Half-reaction of Phenol
Hydroxylase. J. Biol Chem. 260, 5998-6005.
Fitzpatrick, P.F., Ghisla, S. and Massey V. 8-Azidoflavins as Photoaffinity Labels for Flavoproteins.
J. Biol. Chem. 260, 8483-8491.
Stewart, R.C., Hille, R. and Massey V. The Reaction of Arsenite-complexed Xanthine Oxidase with
Oxygen. Evidence for an Oxygen- Reactive Molybdenum Center. J. Biol. Chem. 260, 8892-8904.
Stewart, R.C. and Massey, V. Potentiometric Studies on Native and Flavin- Substituted Old Yellow
Enzyme. J. Biol. Chem. 260, 13639-13647.
Gorelick, R.J., Schopfer, L.M., Ballou, D.P., Massey, V. and Thorpe, C. Interflavin OxidationReduction Reactions between Pig Kidney General Acyl-CoA Dehydrogenase and Electron
Transferring Flavoprotein. Biochemistry 24, 6830-6839.
Surdhar, P.S., Armstrong, D.A., and Massey, V. The One-and-two-electron Reduction of 2thioriboflavin by Radical Anions of CO2 and Dithiothereitol. Can. J. Chem. 64, 67-70.
Massey, V. and Schopfer, L.M. Reactivity of Old Yellow Enzyme with -NADPH and other Pyridine
Nucleotide Derivatives. J. Biol. Chem. 261, 1215-1222.
Hille, R. and Massey, V. The Equilibration of Reducing Equivalents within Milk Xanthine Oxidase.
J. Biol. Chem. 261, 1241-1247.
Ghisla, S., Massey, V. and Yagi, K. Preparation and Some Properties of 6-Substituted Flavins as
Active Site Probes for Flavin Enzymes. Biochemistry 25, 3282-3289.
Miller, S., Ballou, D.P., Massey, V., Williams, C.H. and Walsh, C. Two-electron Reduced Mercuric
Reductase Binds Hg(II) to the Active Site Dithiol but Does Not Catalyze Hg(II) Reduction.
J. Biol. Chem. 261, 2081-2084.
D'Silva, C., Williams, C.H. and Massey, V. Electrophilic Amination of a Single Methionine Residue
Located at the Active Site of D-Amino Acid Oxidase by O-(2,4-Dinitrophenyl) hydroxylamine.
Biochemistry 25, 5602- 5608.
Ghisla, S. and Massey, V. New Flavins for Old: Artificial Flavins as Active Site Probes of
Flavoproteins. Biochem. J. 239, 1-12.
Manstein, D.J., Pai, E.F., Schopfer, L.M. and Massey, V. Absolute Stereochemistry of Flavins in
Enzyme-catalyzed Reactions. Biochemistry 25, 6807-6816.
Anderson, R.F., Hille, R. and Massey, V. The Radical Chemistry of Milk Xanthine Oxidase as
Studied by Radiation Chemistry Techniques. J. Biol. Chem. 261, 15870-15876.
Massey, V., Ghisla, S. and Yagi, K. 6-Azido- and 6-Aminoflavins as Active Site Probes of Flavin
Enzymes. Biochemistry 25, 8095-8102.
Massey, V., Ghisla, S., and Yagi, K. 6-Thiocyanatoflavins and 6-Mercapto flavins as Active Site
Probes of Flavoproteins. Biochemistry 25, 8103- 8112.
Powlowski, J.B., Dagley, S., Massey, V. and Ballou, D.P. Properties of Anthranilate Hydroxylase
(Deaminating), A Flavoprotein from Trichosporon cutaneum. J. Biol. Chem. 262, 69-74.
D'Silva, C., Williams, C.H., Jr. and Massey, V. Identification of Methionine-110 as the Residue
Covalently Modified in the Electrophilic Inactivation of D-Amino-acid Oxidase by 0-(2,4Dinitrophenyl) hydroxylamine. Biochemistry 26, 1717-1722.
Giegel, D.A., Massey, V. and Williams, C.H., Jr. L-Lactate-2-mono-oxygenase: Sequence of Peptides
Containing Residues Modified by 1-Fluoro-2,4-Dinitrobenzene. J. Biol. Chem. 262, 5705-5710.
Entsch, B., Massey, V. and Claiborne, A. para-Hydroxybenzoate Hydroxylase Containing 6Hydroxy-FAD is an Effective Enzyme with Modified Reaction Mechanisms. J. Biol. Chem. 262,
6060-6068.
Negri, A., Massey, V. and Williams, C.H., Jr. D-Aspartate Oxidase from Beef Kidney. J. Biol. Chem.
262, 10026-10034.
Manstein, D.J., Massey, V., Ghisla, S. and Pai, E.F. Stereochemistry and Accessibility of Prostethic
Groups in Flavoproteins. Biochemistry 27, 2300-2305.
Schopfer, L.M., Massey, V., Ghisla, S. and Thorpe, C. Oxidation-Reduction of General Acyl-CoA
Dehydrogenase by the Butryl-CoA/Crotonyl-CoA Couple. A New Investigation of the Rapid
Reaction Kinetics. Biochemistry 27, 6599-6611.
Schopfer, L.M., Massey, V. and Nishino, T. Rapid Reaction Studies on the Reduction and Oxidation
of Chicken Liver Xanthine Dehydrogenase by the Xanthine/Urate and NAD/NADH Couples. J. Biol.
Chem. 263, 13528-13538.
Negri, A., Massey, V., Williams, C.H., Jr. and Schopfer, L.M. The Kinetic Mechanism of Beef
Kidney D-Aspartate Oxidase. J. Biol. Chem. 263, 13557-13563.
Miller, S.M., Moore, M.J., Massey, V., Williams, C.H., Jr., Distefano, M.D., Ballou, D.P. and Walsh,
C.T. Evidence for the Participation of Cys558 and Cys559 at the Active Site of Mercuric Reductase.
Biochemistry 28, 1194-1205.
Nishino, T., Nishino, T., Schopfer, L.M. and Massey, V. The Reactivity of Chicken Liver Xanthine
Dehydrogenase with Molecular Oxygen. J. Biol. Chem. 264, 2518-2527.
Massey 9
(234)
1989
(235)
1989
(236)
1989
(237)
1989
(238)
1989
(239)
1989
(240)
1989
(241)
1989
(242)
1990
(243)
1990
(244)
1990
(245)
1990
(246)
1990
(247)
1990
(248)
1990
(249)
1990
(250)
1991
(251)
1991
(252)
1991
(253)
1991
(254)
1991
(255)
1991
(256)
1991
(257)
1991
(258)
1991
Powlowski, J., Massey, V. and Ballou, D.P. Reactions of Anthranilate Hydroxylase with Salicylate, a
Nonhydroxylated Substrate Analogue. J. Biol. Chem. 264, 5606-5612.
Nishino, T., Nishino, T., Schopfer, L.M. and Massey, V. Reactivity of Chicken Liver Xanthine
Dehydrogenase Containing Modified Flavins. J. Biol. Chem. 264, 6075-6085.
Ghisla, S. and Massey, V. Mechanisms of Flavoprotein-catalyzed Reactions. Eur. J. Biochem. 181, 117.
Einarsdottir, G.H., Stankovich, M.T., Polowski, J., Ballou, D.P. and Massey, V. Regulation of
Oxidation-Reduction Potentials of Anthranilate Hydroxylase from Trichosporon cutaneum by
Substrate and Effector Binding. Biochemistry 28, 4161-4168.
Massey, V., Schopfer, L.M., Nishino, T. and Nishino T. Differences in Protein Structure of Xanthine
Dehydrogenase and Xanthine Oxidase Revealed by Reconstitution with Flavin Active Site Probes. J.
Biol. Chem. 264, 10567-10573.
Brissette, P., Ballou, D.P. and Massey, V. Determination of the Dead Time of a Stopped Flow
Fluorometer. Analytical Biochem. 181, 234-238.
Saito, T., Nishino, T. and Massey, V. Differences in Environment of FAD between NAD-dependent
and O2-dependent Types of Rat Liver Xanthine Dehydrogenase Shown by Active Site Probe Study. J.
Biol. Chem. 164, 15930-15935.
Powlowski, J., Ballou, D.P. and Massey, V. A Rapid Reaction Study of Anthranilate Hydroxylase.
Evidence for a catalytically Important Conformational Change During Slow Initial Turnover with
Anthranilate. J. Biol. Chem. 264, 16008-16016.
Macheroux, P., Kojiro, C.L., Schopfer, L.M., Chakraborty, S., and Massey, V. 19F NMR Studies on
8-Fluoroflavins and 8-Fluoro Flavoproteins. Biochemistry 29, 2670-2679.
Miller, S.M., Massey, V., Ballou, D., Williams, C.H., Jr., Distefano, M.D., Moore, M.J., and Walsh,
C.T. Use of a Site-Directed Triple Mutant to Trap Intermediates: Demonstration that the Flavin
C(4a)-Thiol Adduct and Reduced Flavin are Kinetically Competent Intermediates in Mercuric Ion
Reductase. Biochemistry 29, 2831-2841.
Frederick, K.R., Tung, J., Emerick, R.S., Masiarz, F.R., Chamberlain, S.H., Vasavada, A., Rosenberg,
S., Chakraborty, S., Schopfer, L.M., and Massey, V. Glucose Oxidase from Aspergillus niger.
Cloning, gene sequence, secretion from Saccharomyces cervisiae and kinetic analysis of a yeastderived enzyme. J. Biol. Chem. 265, 3793-3802.
Powlowski, J., Ballou, D.P., and Massey, V. Studies of the Oxidative Half-reaction of Anthranilate
Hydroxylase (Deaminating) with Native and Modified Substrates. J. Biol. Chem. 265, 4969-4975.
Giegel, D.A., Williams, C.H., Jr., and Massey, V. L-Lactate 2-Monooxygenase from Mycobacterium
smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family.
J. Biol. Chem. 265, 6626-6632.
Taylor, M.G. and Massey, V. Decay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase J.
Biol. Chem. 265, 13687-13694.
Ludwig, M.L., Schopfer, L.M., Metzger, A.L., Pattridge, K.A. and Massey, V. Structure and
Oxidation-Reduction Behavior of 1-Deaza-FMN Flavodoxins: Modulation of Redox Potentials in
Flavodoxins. Biochemistry 29, 10364-10375.
Fish, K.M., Massey, V., Sands, R.H., and Dunham, W.R. The Interaction of Bisulfite with Milk
Xanthine Oxidase. J. Biol. Chem. 265, 19665-19671.
Macheroux, P. and Massey, V. 8-Thiocyanatoflavins as Active Site Probes for Flavoproteins.
Biochemistry 30, 456-464.
Miller, S.M., Massey, V., Williams, C.H. Jr., Ballou, D.P. and Walsh, C.T. Communication between
the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.
Biochemistry 30, 2600-2612.
Macheroux, P., Massey, V., Thiele, D.J., and Volokita, M. Expression of Spinach glycolate oxidase in
Saccharomyces cerevisae: purification and characterization. Biochemistry 30, 4612-4619.
Taylor, M.G. and Massey, V. 6-Mercapto-FAD and 6-thiocyanato-FAD as active site probes of
phenol hydroxylase. J. Biol. Chem. 266, 8281-8290.
Taylor, M.G. and Massey, V. Kinetic and isotopic studies of the oxidative half reaction of phenol
hydroxylase. J. Biol. Chem. 266, 8291-8301.
Ermler, V., Ghisla, S., Massey, V. and Schulz, G.E. Structural, spectroscopic and catalytic activity
studies on glutathione reductase reconstituted with FAD analogues. Eur. J. Biochem. 199, 133-138.
Schopfer, L.M., Wessiak, A. and Massey, V. Interpretation of the spectra observed during oxidation
of p-hydroxybenzoate hydroxylase reconstituted with modified flavins. J. Biol. Chem. 266, 1308013085.
Entsch, B., Palfey, B.A., Ballou, D.P. and Massey, V. Catalytic function of tyrosine residues in phydroxybenzoate hydroxylase as determined by the study of site-directed mutants. J. Biol. Chem. 266,
17341-17349.
Hille, R. and Massey, V. The Kinetic behavior of xanthine oxidase containing chemically modified
flavins. J. Biol. Chem. 266, 17401-17408.
Massey 10
(259)
1991
(260)
1991
(261)
1992
(262)
1992
(263)
1992
(264)
1992
(265)
1993
(266)
1993
(267)
1993
(268)
1993
(269)
1993
(270)
1994
(271)
1994
(272)
1994
(273)
1994
(274)
1994
(275)
1994
(276)
1994
(277)
1994
(278)
1994
(279)
1994
(280)
1994
(281)
1994
(282)
1995
(283)
1995
(284)
1995
(285)
1995
Saito, K., Thiele, D.J., Davio, M., Lockridge, O. and Massey, V. The cloning and expression of a
gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis. J. Biol. Chem. 266, 2072020724.
Maeda-Yorita, K., Russell, G.C., Guest, J.R., Massey, V. and Williams, C.H., Jr. Properties of
lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine
nucleotide binding domain. Biochemistry 30, 11788-11795.
Saito, T., Massey, V., and Nishino, T. Light product of photoreactive 6-azido-FAD bound to deflavomilk xanthine oxidase. Biochemistry 31, 6305-6311.
Macheroux, P., Mulrooney, S.B., Williams, C.H., Jr. and Massey, V. Direct expression of active
spinach glycolate oxidase in Escherichia coli. Biochimica et Biophysica Acta 1132, 11-16.
Hunt, J. and Massey, V. Purification and properties of milk xanthine dehydrogenase. J. Biol. Chem.
267, 21479-21485.
Arunachalam, U., Massey, V. and Vaidyanathan, C.S. p-Hydroxyphenylacetate-3-hydroxylase. J.
Biol. Chem. 267, 25848-25855.
Maeda-Yorita, K. and Massey, V. On the Reaction Mechanism of Phenol Hydroxylase. New
Information Obtained by Correlation of Absorbance and Fluorescence Stopped Flow Studies. J. Biol.
Chem. 268, 4134-4144.
Stott, K., Saito, K., Thiele, D. J. and Massey, V. Old Yellow Enzyme. The Discovery of Multiple
Isozymes and a Family of Related Proteins. J. Biol. Chem. 268, 6097-6106.
Xu, F., Mack, C. P., Quandt, K. S., Shlafer, M., Massey, V. and Hultquist, D. E. Pyrroloquinine
Quinone acts with Flavin Reductase to Reduce Ferryl Myoglobin in vitro and protects Isolated Heart
from Reoxygenation Injury. Biochem. Biophys. Res. Commun. 193, 434-439.
Macheroux, P., Kieweg, V., Massey, V., Söderlind, E., Stenberg, K. and Lindqvist, Y. Role of
Tyrosine 129 in the Active Site of Spinach Glycolate Oxidase. Eur. J. Biochem. 213, 1047-1054.
Hunt, J., Massey, V., Dunham, W. R. and Sands, R. H. Redox Potentials of Milk Xanthine
Dehydrogenase. J. Biol. Chem. 268, 18685-18691.
Arunachalam, V., Massey, V. and Miller, S.M. Mechanism of p-Hydroxyphenylacetate-3hydroxylase. A Two-Protein Enzyme. J. Biol. Chem. 269, 150-155.
Palfey, B.A., Entsch, B., Ballou, D.P. and Massey, V. Changes in the Catalytic Properties of pHydroxybenzoate Hydroxylase Caused by the Mutation Asn300Asp. Biochemistry 33, 1545-1554.
Müh, U., Massey, V., and Williams, Jr., C. H. Lactate Monooxygenase. I. Expression of the
Mycobacterial Gene in Escherichia coli and Site-directed Mutagenesis of Lysine 266. J. Biol. Chem.
269, 7982-7988.
Müh, U., Williams, Jr., C. H., and Massey, V. Lactate Monooxygenase. II. Site-directed Mutagenesis
of the Postulated Active Site Base Histidine 290. J. Biol. Chem. 269, 7989-7993.
Müh, U., Williams, Jr., C. H., and Massey, V. Lactate Monooxygenase. III. Additive Contributions of
Active Site Residues to Catalytic Efficiency and Stabilization of an Anionic Transition State. J. Biol.
Chem. 269, 7994-8000.
Arunachalam, U., and Massey, V. Studies on the Oxidative Half-reaction of p-Hydroxyphenylacetate
3-Hydroxylase. J. Biol. Chem. 269, 11795-11801.
Hunt, J., and Massey, V. Studies on the Reductive Half-reaction of Milk Xanthine Dehydrogenase. J.
Biol. Chem. 269, 18904-18914.
Maeda-Yorita, K., Russell, G.C., Guest, J.R., Massey, V., and Williams, C.H. Jr. Modulation of the
Redox Potential of the Flavin in Lipoamide Dehydrogenase from Escherichia coli by Alteration of a
Nearby Charged Residue, K53R. Biochemistry 33, 6213-6220.
Massey, V. Activation of Molecular Oxygen by Flavins and Flavoproteins. J. Biol. Chem. 269,
22459-22462.
Gatti, D.L., Palfey, B.A., Lah, M.S., Entsch, B., Massey, V., Ballou, D.P., and Ludwig, M.L. The
Mobile Flavin of 4-OH Benzoate Hydroxylase. Science 266, 110-114.
Pollegioni, L., Fukui, K., and Massey, V. Studies on the Kinetic Mechanism of Pig Kidney D-Amino
Acid Oxidase by Site-directed Mutagenesis of Tyrosine 224 and Tyrosine 228. J. Biol. Chem. 269,
31666-31673.
Niimura, Y. Yokoyama, K., Ohnishi, K., and Massey, V. A Flavoprotein Functional as NADH
Oxidase form Amphibacillus xylanus Scavenges Hydrogen Peroxide in the Presence of Free FAD.
Biosci. Biotech. Biochem. 58, 2310-2311.
Tedeschi, G., Chen, S., and Massey, V. DT-diaphorase. Redox Potential, Steady-State and Rapid
Reaction Studies. J. Biol. Chem. 270, 1198-1204.
Niino, Y.S., Chakraborty, S., Brown, B.J., and Massey, V. A New Old Yellow Enzyme of
Saccharomyces cerevisiae. J. Biol. Chem. 270, 1983-1991.
Tedeschi, G., Chen, S., and Massey, V. Active Site Studies of DT-diaphorase Employing Artificial
Flavins. J. Biol. Chem. 270, 2512-2516.
Vaz, A.D.N., Chakraborty, S. and Massey, V. Old Yellow Enzyme: Aromatization of Cyclic Enones
and the Mechanism of a Novel Dismutation Reaction. Biochemistry 34, 4246-4256.
Massey 11
(286)
1995
(287)
1995
(288)
1995
(289)
1995
(290)
1995
(291)
1995
(292)
1996
(293)
1996
(294)
1996
(295)
1996
(296)
1996
(297)
1997
(298)
1997
(299)
1997
(300)
1997
(301)
1997
(302)
1997
(303)
1997
(304)
1997
(305)
1997
(306)
1997
(307)
1997
(308)
1997
(309)
1997
(310)
1997
Langkau, B., Vock, P., Massey, V., Fuchs, G. and Ghisla, S. 2-Aminobenzoyl-CoA
Monoxygenase/Reductase. Evidence for Two Distinct Loci Catalyzing Substrate Monooxygenation
and Hydrogenation. Eur. J. Biochem. 230, 676-685.
Tedeschi, G., Deng, P.S.K., Chen, H-H., Forrest, G.L., Massey, V. and Chen, S. A Site-Directed
Mutagenesis Study at Lys-113 of NAD(P)H: Quinone-Acceptor Oxidoreductase: An Involvement of
Lys-113 in the Binding of the Flavin Adenine Dinucleotide Prosthetic Group. Archiv. Biochem.
Biophys. 321, 76-82.
Maeda-Yorita, K., Aki, K., Sagai, H., Misaki, H. and Massey, V. L-Lactate Oxidase and L-Lactate
Monooxygenase: Mechanistic Variations on a Common Structural Theme. Biochimie 77, 631-642.
Niimura, Y, Poole, L.B. and Massey, V. Amphibacillus xylanus NADH Oxidase and Salmonella
Typhimurium Alkyl-hydroperoxide Reductase Flavoprotein Components Show Extremely High
Scavenging Activity for Both Alkyl Hydroperoxide and Hydrogen Peroxide in the presence of S
Typhimurium Alkyl-hydroperoxide Reductase 22-kDa Protein Component. J.Biol.Chem. 270, 2564525650.
Murthy, Y.V.S.N. and Massey, V. Chemical Modification of the N-10 Ribityl Side Chain of Flavins.
Effects on Properties of Flavoprotein Disulfide Oxidoreductases. J. Biol. Chem. 270, 28586-28594.
Karplus, P.A., Fox, K.M. and Massey, V. Structure-function Relations for Old Yellow Enzyme
FASEB. J. 9, 1518-1525.
Sun, W., Williams, C.H. Jr. and Massey, V. Site-directed Mutagenesis of Glycine 99 to Alanine in LLactate Monooxygenase from Mycobacterium smegmatis J. Biol. Chem. 271, 17226-17233.
Raibekas, A. and Massey, V. Glycerol-induced Development of Catalytically Active Conformation of
Crotalus adamanteus L-Amino Acid Oxidase in vitro Proc. Natl. Acad. Sci. (USA) 93, 7546-7551.
Murthy, Y.V.S.N. and Massey, V. 19F NMR Studies with 21-F-21-deoxyarabinoflavoproteins. J. Biol.
Chem 271, 19915-19921.
Yorita, K., Aki, K., Ohkuma-Soyejima, T., Kokubo, T., Misaki, H. and Massey, V. Conversion of LLactate Oxidase to a Long Chain -Hydroxyacid Oxidase by Site-directed Mutagenesis of Alanine 95
to Glycine. J. Biol. Chem 271, 28300-28305.
Niimura, Y. and Massey, V. Reaction Mechanism of Amphibacillus xylanus NADH Oxidase/Alkyl
hydroperoxide Reductase Flavoprotein. J. Biol. Chem. 271, 30459-30464.
Benson, T.E., Walsh, C.T. and Massey, V. Kinetic Characterization of Wild Type and S229A Mutant
Mur B: Evidence for the Role of Ser 229 as a General Acid. Biochemistry 36, 696-805.
Harris, C.M. and Massey, V. The Reaction of Reduced Xanthine Dehydrogenase with Molecular
Oxygen. Reaction Kinetics and Measurement of Superoxide Radical. J. Biol. Chem 272, 8370-8379.
Chaiyen, P., Brissette, P., Ballou, D.P. and Massey, V. Thermodynamics and Reduction Kinetics of 2Methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Biochemistry 36, 2612-2621.
Chaiyen, P., Brissette, P., Ballou, D.P. and Massey, V., Unusual mechanism of oxygen atom transfer
and product rearrangement in the catalytic reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid
oxygenase. Biochemistry 36, 8060-8070.
Chaiyen, P., Ballou, D.P. and Massey, V. Gene cloning, sequence analysis, and expression of 2methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Proc. Natl. Acad. Sci. USA 94, 7233-7238.
Raibekas, A.A., and Massey, V. Glycerol-assisted restorative adjustment of flavoenzyme
conformation perturbed by site-directed mutagenesis. J. Biol. Chem 272, 22248-22252.
Harris, C.M., and Massey, V. Kinetic isotope effects and electron transfer in the reduction of xanthine
oxidoreductase with 4-hydroxypyrimidine J. Biol. Chem 272, 22514-22525.
Yorita, K., Janko, K., Aki, K., Ghisla, S., Palfey, B.A., and Massey, V. On the reaction mechanism of
L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted
mandelates. Proc. Natl. Acad. Sci. USA 94, 9590-9595.
Sun, W., Williams, C.H. Jr., and Massey, V. On the role of Glycine 99 in L-lactate monooxygenase
from Mycobacterium smegmatis. J. Biol. Chem 272, 27065-27076.
Chaiyen, P., Brissette, P., Ballou, D.P. and Massey, V. Reaction of 2-methyl-3-hydroxypyridine-5carboxylic acid (MHPC) oxygenase with N-methyl-5-hydroxynicotinic acid: Studies on the mode of
binding and protonation status of the substrate. Biochemistry 36, 13856-13864.
Harris, C.M. and Massey, V. The oxidative half reaction of xanthine dehydrogenase with NAD,
reaction kinetics and steady state mechanism. J. Biol. Chem. 272, 28335-28341.
Palfey, B.A., Ballou, D.P. and Massey, V. Flavin conformational changes in the catalytic cycle of phydroxybenzoate hydroxylase substituted with 6-azido and 6-aminoflavin adenine dinucleotide.
Biochemistry 36, 15713-15723.
Massey, V. and Harris C.M. Milk xanthine oxidoreductase: the first one hundred years. Biochem. Soc.
Transactions 25, 750-755.
Nishiyama, Y., Massey, V., Anzai, Y., Watanabe, T., Miyaji, T., Uchimura, T., Kozake, M., Suzuki,
H. and Niimura Y. Purification and Characterization of Sporolactobacillus inulinus NADH oxidase
and its physiological role in aerobic metabolism of the bacterium. J. Fermentation and
Bioengineering 84, 22-27.
Massey 12
(311)
1998
(312)
1998
(313)
1998
(314)
1998
(315)
1998
(316)
1998
(317)
1999
(318)
1999
(319)
1999
(320)
1999
(321)
1999
(322)
1999
(323)
1999
(324)
1999
(325)
2000
(326)
2000
(327)
2000
(328)
2000
(329)
2000
(330)
2000
(331)
2001
(332)
2001
(333)
2001
(334)
2001
(335)
2001
(336)
2001
Murthy, Y.V.S.N, and Massey, V. Synthesis and properties of 8-CN-flavin nucleotide analogs and
studies with flavoproteins. J. Biol. Chem. 373, 8975-8982.
Koyama, N., Koitabashi, T., Niimura, Y. and Massey, V. Peroxide reductase activity of NADH
dehydrogenase of an alkaphilic bacillus in the presence of a 22-kDa protein component from
Amphibacillus xylanus. Biochem. Biophys Res. Commun. 247, 659-662.
Raibekas, A.A. and Massey, V. Primary structure of the snake venom L-amino acid oxidase shows
high homology with the mouse B cell interleukin 4-induced Fig 1 protein. Biochem. Biophys. Res.
Commun. 248, 476-478.
Morimoto, Y., Yorita, K., Aki, K., Misaki, H. and Massey, V. L-lactate oxidase from Aerococcus
viridans crystallized as an octamer. Preliminary x-ray studies. Biochemie 80, 309-312.
Brown, B. J., Deng, Z., Karplus, P. A., and Massey, V. On the active site of old yellow enzyme. Role
of histidine 191 and asparagine 194. J. Biol. Chem. 273, 32753-32762.
Kohli, R. M. and Massey, V. The oxidative half-reaction of old yellow enzyme. The role of tyrosine
196. J. Biol. Chem. 273, 32763-32770.
Palfey, B.A., Moran G.R., Entsch, B., Ballou, D.B., and Massey, V. Substrate recognition by
"Password" in p-hydroxybenzoate hydroxylase. Biochemistry 38, 1153-1158..
Harris, C.M., Sanders, S.A. and Massey, V. Role of the flavin midpoint potential and NAD binding in
determining NAD versus oxygen reactivity of xanthine oxidoreductase. J. Biol. Chem. 274, 45614569.
Xu, D., Kohli, R. M., and Massey, V. The role of threonine 37 in flavin reactivity of the old yellow
enzyme. Proc. Natl. Acad. Sci. 96 3556-3561.
Murthy, Y. V. S. N., Meah, Y. and Massey, V. Conversion of a flavoprotein reductase to a desaturase
by manipulation of the flavin redox potential. J. Am. Chem. Soc. 121 5344-5345.
Ortiz-Maldonado, M., Ballou, D. P. and Massey, V. Use of free energy relationships to probe the
individual steps of hydroxylation of p-hydroxybenzoate hydroxylase: studies with a series of 8substituted flavins. Biochemistry 38 8124-8137.
Sanders, S. A., Williams, C. H. and Massey, V. The roles of two amino acid residues in the active site
of L-lactate monooxygenase. Mutation of arginine 187 to methionine and histidine 240 to glutamine.
J. Biol. Chem. 274, 22289-22295.
Sanders, S. A. and Massey, V. The thermodynamics of xanthine oxidoreductase catalysis.
Antioxidants & Redox Signaling 1, 371-379.
Ortiz-Maldonado, M., Gatti, D., Ballou, D. P. and Massey, V. Structure-function correlations of the
reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a
series of 8-substituted flavins Biochemistry 38, 16636-16647.
Yorita, K., Misaki, H., Palfey, B. A. and Massey, V. On the interpretation of quantitative structurefunction activity relationship data for L-lactate oxidase. Proc. Natl. Acad. Sci. USA 97, 2480-2485.
Raibekas, A. A., Fukui, K. and Massey, V. Design and properties of human D-amino acid oxidase
with covalently attached flavin. Proc. Natl. Acad. Sci. USA 97, 3089-3093.
Massey, V. The chemical and biological versatility of riboflavin. Biochem. Soc. Transactions 28, 283296.
Niimura, Y., Nishiyama, Y., Saito, D., Tsuji, H., Hikada, M., Miyaji, T., Watanabe, T. and Massey,
V. A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase
in Amphibacillus xylanus. J. Bact. 182, 5046-5051.
Meah, Y. and Massey, V. Old yellow enzyme: stepwise reduction of nitroolefins and catalysis of acinitro tautomerization. Proc. Natl. Acad. Sci. USA 97, 10733-10738.
Yorita, K., Matsuoka, T., Misaki, H. and Massey, V. Interaction of two arginine residues in lactate
oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN. Proc. Natl. Acad. Sci. USA
97, 13039-13044.
Ortiz-Maldonado, M., Ballou, D. P. and Massey, V. A rate limiting conformational change of the
flavin in p-hydroxybenzoate hydroxylase is necessary for ligand exchange and catalysis: studies with
8-mercapto- and 8-hydroxy-flavins. Biochemistry 40, 1091-1101.
Nishiyama, Y., Massey, V., Takeda, K., Kawasaki, S., Sato, J., Watanabe, T. anad Niimura, Y.
Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family:
existence and physiological role in bacteria. J. Bact. 183, 2431-2438.
Ortiz-Maldonado, M., Aeschliman, S. M., Ballou, D. P. and Massey, V. Synergistic interactions of
multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase:
studies of the Lys 297 Met, Asn 300Asp and Tyr 385 Phe mutants reconstituted with 8-Cl-flavin.
Biochemistry 40, 8705-8716,.
Meah, Y., Brown, B. J., Chakraborty, S. and Massey, V. Old Yellow Enzyme: reduction of nitrate
esters, glycerin trinitrate and 1,2-propylene dinitrate. Proc. Natl. Acad. Sci. USA, subm98, 8560-8565.
Xu, D., Ballou, D. P. and Massey, V. Studies on the mechanism of phenol hydroxylase: mutants
Tyr289Phe, Asp54Asn and Arg281 Met. Biochemistry, 40, 12369-12378.
Sheng, D., Ballou, D. P. and Massey, V. Mechanistic studies of cyclohexanone monoxygenase:
chemical properties of intermediates involved in catalysis. Biochemistry, 40, 11156-11167.
Massey 13
(337)
2001
(338)
2001
(339)
2001
(340)
2002
(341)
2002
(342)
2002
(343)
2003
(344)
2003
Zheng, Y., Massey, V., Schaller, A., Palfey, B. A. and Carey, P. R. Comparison of resonance Raman
spectra of flavin-3.4-dihydroxybenzoate charge-transfer complexes in three flavoenzymes. J. Raman
Spectroscopy , 32, 579-586.
Salomon, M., Eisenreich, W., Dürr, H., Schleicher, E., Knieb, E., Massey, V., Rüdiger, W., Müller,
F., Bacher, A. and Richter, G. An optomechanical transducer in the blue light receptor phototropin
from Avena sativa. Proc. Natl. Acad. Sci, USA, 98, 12357-12361.
Brown, B. J., Hyun, J-W., Duvveri, S., Karplus, P. A. and Massey, V. The role of glutamine 114 in
Old Yellow Enzyme. J Biol Chem , 277, 2138-2145.
Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL, Protein and ligand dynamics
in 4-hydroxybenzoate hydroxylase.Proc Natl Acad Sci U S A, 99, 608-613.
Chakraborty S, Massey V. Reaction of reduced flavins and flavoproteins with diphenyliodonium
chloride, J Biol Chem , 277, 41507-41516.
Xu D, Enroth C, Lindqvist Y, Ballou DP, Massey V. Studies of the mechanism of phenol
hydroxylase: effect of mutation of proline 364 to serine, Biochemistry, 41, 13627-13636.
Palfey BA, Murthy YV, Massey V, Altered balance of half-reactions in p-hydroxybenzoate
hydroxylase caused by substituting the 2'-carbon of FAD with fluorine, J Biol Chem. (in the press).
Bauer, H., Massey, V., Arscott, L.D., Schirmer, R.H., Ballou, D.P. and Williams, C.H., Jr. The
Mechanism of high Mr thioredoxin reductase from Drosophila melanogaster. J. Biol. Chem. Accepted
pending 2 changes, 16 May 2003.
Massey 14