| Year |
Citation |
Score |
| 2005 |
Brender JR, Dertouzos J, Ballou DP, Massey V, Palfey BA, Entsch B, Steel DG, Gafni A. Conformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: single-molecule studies. Journal of the American Chemical Society. 127: 18171-8. PMID 16366570 DOI: 10.1021/Ja055171O |
0.612 |
|
| 2004 |
Chaiyen P, Sucharitakul J, Svasti J, Entsch B, Massey V, Ballou DP. Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Biochemistry. 43: 3933-43. PMID 15049701 DOI: 10.1021/Bi035734D |
0.774 |
|
| 2003 |
Bauer H, Massey V, Arscott LD, Schirmer RH, Ballou DP, Williams CH. The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster. The Journal of Biological Chemistry. 278: 33020-8. PMID 12816954 DOI: 10.1074/Jbc.M303762200 |
0.766 |
|
| 2003 |
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. The Journal of Biological Chemistry. 278: 22210-6. PMID 12684497 DOI: 10.1074/Jbc.M301830200 |
0.453 |
|
| 2002 |
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: 13627-36. PMID 12427024 DOI: 10.1021/Bi020446N |
0.698 |
|
| 2002 |
Chakraborty S, Massey V. Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride. The Journal of Biological Chemistry. 277: 41507-16. PMID 12186866 DOI: 10.1074/Jbc.M205432200 |
0.49 |
|
| 2002 |
Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL. Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase. Proceedings of the National Academy of Sciences of the United States of America. 99: 608-13. PMID 11805318 DOI: 10.1073/Pnas.022640199 |
0.822 |
|
| 2002 |
Brown BJ, Hyun JW, Duvvuri S, Karplus PA, Massey V. The role of glutamine 114 in old yellow enzyme. The Journal of Biological Chemistry. 277: 2138-45. PMID 11668181 DOI: 10.1074/Jbc.M108453200 |
0.481 |
|
| 2001 |
Xu D, Ballou DP, Massey V. Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry. 40: 12369-78. PMID 11591156 DOI: 10.1021/Bi010962Y |
0.714 |
|
| 2001 |
Sheng D, Ballou DP, Massey V. Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry. 40: 11156-67. PMID 11551214 DOI: 10.1021/Bi011153H |
0.62 |
|
| 2001 |
Ortiz-Maldonado M, Aeschliman SM, Ballou DP, Massey V. Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin. Biochemistry. 40: 8705-16. PMID 11467930 DOI: 10.1021/Bi010892V |
0.823 |
|
| 2001 |
Meah Y, Brown BJ, Chakraborty S, Massey V. Old yellow enzyme: reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate. Proceedings of the National Academy of Sciences of the United States of America. 98: 8560-5. PMID 11438708 DOI: 10.1073/Pnas.151249098 |
0.533 |
|
| 2001 |
Nishiyama Y, Massey V, Takeda K, Kawasaki S, Sato J, Watanabe T, Niimura Y. Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria. Journal of Bacteriology. 183: 2431-8. PMID 11274101 DOI: 10.1128/Jb.183.8.2431-2438.2001 |
0.368 |
|
| 2001 |
Ortiz-Maldonado M, Ballou DP, 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: 1091-101. PMID 11170433 DOI: 10.1021/Bi002139S |
0.836 |
|
| 2000 |
Yorita K, Matsuoka T, Misaki H, Massey V. Interaction of two arginine residues in lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN. Proceedings of the National Academy of Sciences of the United States of America. 97: 13039-44. PMID 11078532 DOI: 10.1073/Pnas.250472297 |
0.505 |
|
| 2000 |
Meah Y, Massey V. Old yellow enzyme: stepwise reduction of nitro-olefins and catalysis of aci-nitro tautomerization. Proceedings of the National Academy of Sciences of the United States of America. 97: 10733-8. PMID 10995477 DOI: 10.1073/Pnas.190345597 |
0.514 |
|
| 2000 |
Massey V. The chemical and biological versatility of riboflavin. Biochemical Society Transactions. 28: 283-96. PMID 10961912 DOI: 10.1042/Bst0280283 |
0.44 |
|
| 2000 |
Niimura Y, Nishiyama Y, Saito D, Tsuji H, Hidaka M, Miyaji T, Watanabe T, Massey V. A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus. Journal of Bacteriology. 182: 5046-51. PMID 10960086 DOI: 10.1128/Jb.182.18.5046-5051.2000 |
0.461 |
|
| 2000 |
Raibekas AA, Fukui K, Massey V. Design and properties of human D-amino acid oxidase with covalently attached flavin. Proceedings of the National Academy of Sciences of the United States of America. 97: 3089-93. PMID 10716694 DOI: 10.1073/Pnas.97.7.3089 |
0.463 |
|
| 2000 |
Yorita K, Misaki H, Palfey BA, Massey V. On the interpretation of quantitative structure-function activity relationship data for lactate oxidase. Proceedings of the National Academy of Sciences of the United States of America. 97: 2480-5. PMID 10706608 DOI: 10.1073/Pnas.040559797 |
0.493 |
|
| 1999 |
Sanders SA, Massey V. The thermodynamics of xanthine oxidoreductase catalysis. Antioxidants & Redox Signaling. 1: 371-9. PMID 11229448 DOI: 10.1089/Ars.1999.1.3-371 |
0.472 |
|
| 1999 |
Ortiz-Maldonado M, Gatti D, Ballou DP, 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: 16636-47. PMID 10600126 DOI: 10.1021/Bi991603U |
0.804 |
|
| 1999 |
Sanders SA, Williams CH, 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. The Journal of Biological Chemistry. 274: 22289-95. PMID 10428797 DOI: 10.1074/Jbc.274.32.22289 |
0.714 |
|
| 1999 |
Ortiz-Maldonado M, Ballou DP, Massey V. Use of free energy relationships to probe the individual steps of hydroxylation of p-hydroxybenzoate hydroxylase: studies with a series of 8-substituted flavins. Biochemistry. 38: 8124-37. PMID 10387058 DOI: 10.1021/Bi990560E |
0.792 |
|
| 1999 |
Xu D, Kohli RM, Massey V. The role of threonine 37 in flavin reactivity of the old yellow enzyme. Proceedings of the National Academy of Sciences of the United States of America. 96: 3556-61. PMID 10097075 DOI: 10.1073/Pnas.96.7.3556 |
0.594 |
|
| 1999 |
Harris CM, Sanders SA, Massey V. Role of the flavin midpoint potential and NAD binding in determining NAD versus oxygen reactivity of xanthine oxidoreductase. The Journal of Biological Chemistry. 274: 4561-9. PMID 9988690 DOI: 10.1074/Jbc.274.8.4561 |
0.448 |
|
| 1999 |
Palfey BA, Moran GR, Entsch B, Ballou DP, Massey V. Substrate recognition by "password" in p-hydroxybenzoate hydroxylase. Biochemistry. 38: 1153-8. PMID 9930974 DOI: 10.1021/Bi9826613 |
0.739 |
|
| 1999 |
Murthy YVSN, Meah Y, Massey V. Conversion of a flavoprotein reductase to a desaturase by manipulation of the flavin redox potential Journal of the American Chemical Society. 121: 5344-5345. DOI: 10.1021/Ja990908T |
0.353 |
|
| 1999 |
Palfey BA, Moran GR, Entsch B, Ballou DP, Massey V. Substrate recognition by "password" in p-hydroxybenzoate hydroxylase Biochemistry. 38: x-1158. |
0.673 |
|
| 1998 |
GIBSON QH, MASSEY V, ATHERTON NM. The nature of compounds present in mixtures of oxidized and reduced flavin mononucleotides. The Biochemical Journal. 85: 369-83. PMID 13947737 DOI: 10.1042/Bj0850369 |
0.55 |
|
| 1998 |
MASSEY V, GIBSON QH, VEEGER C. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). The Biochemical Journal. 77: 341-51. PMID 13767908 DOI: 10.1042/bj0770341 |
0.544 |
|
| 1998 |
Kohli RM, Massey V. The oxidative half-reaction of Old Yellow Enzyme. The role of tyrosine 196. The Journal of Biological Chemistry. 273: 32763-70. PMID 9830020 DOI: 10.1074/Jbc.273.49.32763 |
0.509 |
|
| 1998 |
Brown BJ, Deng Z, Karplus PA, Massey V. On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194. The Journal of Biological Chemistry. 273: 32753-62. PMID 9830019 DOI: 10.1074/Jbc.273.49.32753 |
0.494 |
|
| 1998 |
Raibekas AA, Massey V. Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein. Biochemical and Biophysical Research Communications. 248: 476-8. PMID 9703950 DOI: 10.1006/Bbrc.1998.9024 |
0.318 |
|
| 1998 |
Morimoto Y, Yorita K, Aki K, Misaki H, Massey V. L-lactate oxidase from Aerococcus viridans crystallized as an octamer. Preliminary X-ray studies. Biochimie. 80: 309-12. PMID 9672750 DOI: 10.1016/S0300-9084(98)80072-2 |
0.321 |
|
| 1998 |
Koyama N, Koitabashi T, Niimura Y, Massey V. Peroxide reductase activity of NADH dehydrogenase of an alkaliphilic Bacillus in the presence of a 22-kDa protein component from Amphibacillus xylanus. Biochemical and Biophysical Research Communications. 247: 659-62. PMID 9647749 DOI: 10.1006/Bbrc.1998.8749 |
0.398 |
|
| 1998 |
Murthy YV, Massey V. Synthesis and properties of 8-CN-flavin nucleotide analogs and studies with flavoproteins. The Journal of Biological Chemistry. 273: 8975-82. PMID 9535883 DOI: 10.1074/Jbc.273.15.8975 |
0.511 |
|
| 1997 |
Palfey BA, Ballou DP, Massey V. Flavin conformational changes in the catalytic cycle of p-hydroxybenzoate hydroxylase substituted with 6-azido- and 6-aminoflavin adenine dinucleotide. Biochemistry. 36: 15713-23. PMID 9398300 DOI: 10.1021/Bi971427U |
0.658 |
|
| 1997 |
Chaiyen P, Brissette P, Ballou DP, Massey V. Reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase with N-methyl-5-hydroxynicotinic acid: studies on the mode of binding, and protonation status of the substrate. Biochemistry. 36: 13856-64. PMID 9374863 DOI: 10.1021/Bi9715122 |
0.744 |
|
| 1997 |
Harris CM, Massey V. The oxidative half-reaction of xanthine dehydrogenase with NAD; reaction kinetics and steady-state mechanism. The Journal of Biological Chemistry. 272: 28335-41. PMID 9353290 DOI: 10.1074/Jbc.272.45.28335 |
0.444 |
|
| 1997 |
Sun W, Williams CH, Massey V. The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis. The Journal of Biological Chemistry. 272: 27065-76. PMID 9341146 DOI: 10.1074/Jbc.272.43.27065 |
0.703 |
|
| 1997 |
Harris CM, Massey V. Kinetic isotope effects and electron transfer in the reduction of xanthine oxidoreductase with 4-hydroxypyrimidine. A comparison between oxidase and dehydrogenase forms. The Journal of Biological Chemistry. 272: 22514-25. PMID 9278404 DOI: 10.1074/Jbc.272.36.22514 |
0.422 |
|
| 1997 |
Yorita K, Janko K, Aki K, Ghisla S, Palfey BA, Massey V. On the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates. Proceedings of the National Academy of Sciences of the United States of America. 94: 9590-5. PMID 9275167 DOI: 10.1073/Pnas.94.18.9590 |
0.347 |
|
| 1997 |
Raibekas AA, Massey V. Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis. The Journal of Biological Chemistry. 272: 22248-52. PMID 9268372 DOI: 10.1074/Jbc.272.35.22248 |
0.386 |
|
| 1997 |
Murthy YV, Massey V. Syntheses and applications of flavin analogs as active site probes for flavoproteins. Methods in Enzymology. 280: 436-60. PMID 9211339 DOI: 10.1016/S0076-6879(97)80135-8 |
0.391 |
|
| 1997 |
Chaiyen P, Ballou DP, Massey V. Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Proceedings of the National Academy of Sciences of the United States of America. 94: 7233-8. PMID 9207074 DOI: 10.1073/Pnas.94.14.7233 |
0.721 |
|
| 1997 |
Chaiyen P, Brissette P, Ballou DP, 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: 8060-70. PMID 9201954 DOI: 10.1021/Bi970089U |
0.74 |
|
| 1997 |
Harris CM, Massey V. The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical. The Journal of Biological Chemistry. 272: 8370-9. PMID 9079661 DOI: 10.1074/Jbc.272.13.8370 |
0.423 |
|
| 1997 |
Chaiyen P, Brissette P, Ballou DP, Massey V. Thermodynamics and reduction kinetics properties of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Biochemistry. 36: 2612-21. PMID 9054568 DOI: 10.1021/Bi962325R |
0.76 |
|
| 1997 |
Benson TE, Walsh CT, Massey V. Kinetic characterization of wild-type and S229A mutant MurB: evidence for the role of Ser 229 as a general acid. Biochemistry. 36: 796-805. PMID 9020777 DOI: 10.1021/Bi962220O |
0.465 |
|
| 1997 |
Nishiyama Y, Massey V, Anzai Y, Watanabe T, Miyaji T, Uchimura T, Kozaki M, Suzuki H, Niimura Y. Purification and characterization of Sporolactobacillus inulinus NADH oxidase and its physiological role in aerobic metabolism of the bacterium Journal of Fermentation and Bioengineering. 84: 22-27. DOI: 10.1016/S0922-338X(97)82781-X |
0.369 |
|
| 1997 |
Palfey BA, Moran G, Entsch B, Ballou DP, Massey V. Flavin movement during the reductive half-reaction of p-hydroxybenzoate hydroxylase Faseb Journal. 11: A853. |
0.494 |
|
| 1996 |
Niimura Y, Massey V. Reaction mechanism of Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein. The Journal of Biological Chemistry. 271: 30459-64. PMID 8940011 DOI: 10.1074/Jbc.271.48.30459 |
0.49 |
|
| 1996 |
Yorita K, Aki K, Ohkuma-Soyejima T, Kokubo T, Misaki H, Massey V. Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine. The Journal of Biological Chemistry. 271: 28300-5. PMID 8910450 DOI: 10.1074/Jbc.271.45.28300 |
0.401 |
|
| 1996 |
Raibekas AA, Massey V. Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro. Proceedings of the National Academy of Sciences of the United States of America. 93: 7546-51. PMID 8755511 DOI: 10.1073/Pnas.93.15.7546 |
0.402 |
|
| 1996 |
Murthy YVSN, Massey V. 19F NMR studies with 2'-F-2'-deoxyarabinoflavoproteins. The Journal of Biological Chemistry. 271: 19915-21. PMID 8702705 DOI: 10.1074/Jbc.271.33.19915 |
0.352 |
|
| 1996 |
Sun W, Williams CH, Massey V. Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis. The Journal of Biological Chemistry. 271: 17226-33. PMID 8663383 DOI: 10.1074/Jbc.271.29.17226 |
0.687 |
|
| 1996 |
Deng Z, Karplus PA, Massey V. Crystallographic studies of lactate monooxygenase (LMO) and old yellow enzyme 2 (OYE2) Acta Crystallographica Section a Foundations of Crystallography. 52: C117-C118. DOI: 10.1107/S0108767396094469 |
0.323 |
|
| 1995 |
Maeda-Yorita K, Aki K, Sagai H, Misaki H, Massey V. L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme. Biochimie. 77: 631-42. PMID 8589073 DOI: 10.1016/0300-9084(96)88178-8 |
0.497 |
|
| 1995 |
Niino YS, Chakraborty S, Brown BJ, Massey V. A new old yellow enzyme of Saccharomyces cerevisiae. The Journal of Biological Chemistry. 270: 1983-91. PMID 7836424 DOI: 10.1074/Jbc.270.5.1983 |
0.403 |
|
| 1995 |
Tedeschi G, Chen S, Massey V. DT-diaphorase. Redox potential, steady-state, and rapid reaction studies. The Journal of Biological Chemistry. 270: 1198-204. PMID 7836380 DOI: 10.1074/Jbc.270.3.1198 |
0.49 |
|
| 1995 |
Vaz AD, Chakraborty S, Massey V. Old Yellow enzyme: aromatization of cyclic enones and the mechanism of a novel dismutation reaction. Biochemistry. 34: 4246-56. PMID 7703238 DOI: 10.1021/Bi00013A014 |
0.346 |
|
| 1995 |
Tedeschi G, Deng PS, Chen HH, Forrest GL, Massey V, 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. Archives of Biochemistry and Biophysics. 321: 76-82. PMID 7639539 DOI: 10.1006/Abbi.1995.1370 |
0.441 |
|
| 1995 |
Langkau B, Vock P, Massey V, Fuchs G, Ghisla S. 2-Aminobenzoyl-CoA monooxygenase/reductase. Evidence for two distinct loci catalyzing substrate monooxygenation and hydrogenation. European Journal of Biochemistry / Febs. 230: 676-85. PMID 7607242 DOI: 10.1111/j.1432-1033.1995.tb20609.x |
0.38 |
|
| 1995 |
Niimura Y, Poole LB, 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. The Journal of Biological Chemistry. 270: 25645-50. PMID 7592740 DOI: 10.1074/Jbc.270.43.25645 |
0.419 |
|
| 1995 |
Tedeschi G, Chen S, Massey V. Active site studies of DT-diaphorase employing artificial flavins. The Journal of Biological Chemistry. 270: 2512-6. PMID 7531691 DOI: 10.1074/Jbc.270.6.2512 |
0.518 |
|
| 1995 |
Murthy YV, Massey V. Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases. The Journal of Biological Chemistry. 270: 28586-94. PMID 7499374 DOI: 10.1074/Jbc.270.48.28586 |
0.427 |
|
| 1995 |
Langkau B, Vock P, Massey V, Fuchs G, Ghisla S. 2-Aminobenzoyl-CoA Monooxygenase/Reductase Febs Journal. 230: 676-685. DOI: 10.1111/J.1432-1033.1995.0676H.X |
0.478 |
|
| 1994 |
Palfey BA, Entsch B, Ballou DP, Massey V. Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp. Biochemistry. 33: 1545-54. PMID 8312275 DOI: 10.1021/Bi00172A035 |
0.674 |
|
| 1994 |
Arunachalam U, Massey V, Miller SM. Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme. The Journal of Biological Chemistry. 269: 150-5. PMID 8276789 |
0.403 |
|
| 1994 |
Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH. Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R. Biochemistry. 33: 6213-20. PMID 8193135 DOI: 10.1021/Bi00186A022 |
0.726 |
|
| 1994 |
Arunachalam U, Massey V. Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase. The Journal of Biological Chemistry. 269: 11795-801. PMID 8163477 |
0.309 |
|
| 1994 |
Müh U, Williams CH, Massey V. Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition state. The Journal of Biological Chemistry. 269: 7994-8000. PMID 8132520 |
0.709 |
|
| 1994 |
Müh U, Williams CH, Massey V. Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290. The Journal of Biological Chemistry. 269: 7989-93. PMID 8132519 |
0.708 |
|
| 1994 |
Müh U, Massey V, Williams CH. Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266. The Journal of Biological Chemistry. 269: 7982-8. PMID 8132518 |
0.706 |
|
| 1994 |
Hunt J, Massey V. Studies of the reductive half-reaction of milk xanthine dehydrogenase. The Journal of Biological Chemistry. 269: 18904-14. PMID 8034647 |
0.326 |
|
| 1994 |
Pollegioni L, Fukui K, Massey V. Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228. The Journal of Biological Chemistry. 269: 31666-73. PMID 7989339 |
0.423 |
|
| 1994 |
Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML. The mobile flavin of 4-OH benzoate hydroxylase. Science (New York, N.Y.). 266: 110-4. PMID 7939628 DOI: 10.1126/Science.7939628 |
0.645 |
|
| 1994 |
Niimura Y, Yokoyama K, Ohnishi K, Massey V. A flavoprotein functional as nadh oxidase from amphibacillus xylanus scavenges hydrogen peroxide in the presence of free fad Bioscience, Biotechnology and Biochemistry. 58: 2310-2311. DOI: 10.1271/Bbb.58.2310 |
0.396 |
|
| 1993 |
Macheroux P, Kieweg V, Massey V, Söderlind E, Stenberg K, Lindqvist Y. Role of tyrosine 129 in the active site of spinach glycolate oxidase. European Journal of Biochemistry / Febs. 213: 1047-54. PMID 8504801 DOI: 10.1111/J.1432-1033.1993.Tb17852.X |
0.462 |
|
| 1993 |
Stott K, Saito K, Thiele DJ, Massey V. Old Yellow Enzyme. The discovery of multiple isozymes and a family of related proteins. The Journal of Biological Chemistry. 268: 6097-106. PMID 8454584 |
0.363 |
|
| 1993 |
Maeda-Yorita K, Massey V. On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies. The Journal of Biological Chemistry. 268: 4134-44. PMID 8440702 |
0.346 |
|
| 1993 |
Xu F, Mack CP, Quandt KS, Shlafer M, Massey V, Hultquist DE. Pyrroloquinoline quinone acts with flavin reductase to reduce ferryl myoglobin in vitro and protects isolated heart from re-oxygenation injury. Biochemical and Biophysical Research Communications. 193: 434-9. PMID 8389151 DOI: 10.1006/Bbrc.1993.1642 |
0.323 |
|
| 1992 |
Saito T, Massey V, Nishino T. Light product of photoreactive 6-azido-FAD bound to deflavo-milk xanthine oxidase. Biochemistry. 31: 6305-11. PMID 1627569 DOI: 10.1021/Bi00142A020 |
0.38 |
|
| 1992 |
Arunachalam U, Massey V, Vaidyanathan CS. p-Hydroxyphenylacetate-3-hydroxylase. A two-protein component enzyme. The Journal of Biological Chemistry. 267: 25848-55. PMID 1464599 |
0.334 |
|
| 1992 |
Hunt J, Massey V. Purification and properties of milk xanthine dehydrogenase. The Journal of Biological Chemistry. 267: 21479-85. PMID 1328233 |
0.395 |
|
| 1992 |
Macheroux P, Mulrooney SB, Williams CH, Massey V. Direct expression of active spinach glycolate oxidase in Escherichia coli. Biochimica Et Biophysica Acta. 1132: 11-6. PMID 1324737 DOI: 10.1016/0167-4781(92)90046-3 |
0.66 |
|
| 1991 |
Ermler U, Ghisla S, Massey V, Schulz GE. Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues. European Journal of Biochemistry / Febs. 199: 133-8. PMID 2065668 DOI: 10.1111/J.1432-1033.1991.Tb16100.X |
0.399 |
|
| 1991 |
Taylor MG, Massey V. Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase. The Journal of Biological Chemistry. 266: 8291-301. PMID 2022646 |
0.634 |
|
| 1991 |
Taylor MG, Massey V. 6-Mercapto-FAD and 6-thiocyanato-FAD as active site probes of phenol hydroxylase. The Journal of Biological Chemistry. 266: 8281-90. PMID 2022645 |
0.683 |
|
| 1991 |
Miller SM, Massey V, Williams CH, Ballou DP, Walsh CT. Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis. Biochemistry. 30: 2600-12. PMID 2001350 DOI: 10.1021/Bi00224A006 |
0.769 |
|
| 1991 |
Saito K, Thiele DJ, Davio M, Lockridge O, Massey V. The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis. The Journal of Biological Chemistry. 266: 20720-4. PMID 1939123 |
0.314 |
|
| 1991 |
Entsch B, Palfey BA, Ballou DP, Massey V. Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants. The Journal of Biological Chemistry. 266: 17341-9. PMID 1910043 |
0.635 |
|
| 1991 |
Hille R, Massey V. The kinetic behavior of xanthine oxidase containing chemically modified flavins. The Journal of Biological Chemistry. 266: 17401-8. PMID 1894627 |
0.736 |
|
| 1991 |
Macheroux P, Massey V, Thiele DJ, Volokita M. Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: purification and characterization. Biochemistry. 30: 4612-9. PMID 1850628 DOI: 10.1021/Bi00232A036 |
0.388 |
|
| 1991 |
Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH. Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. Biochemistry. 30: 11788-95. PMID 1751496 DOI: 10.1021/Bi00115A008 |
0.726 |
|
| 1991 |
Macheroux P, Massey V. 8-thiocyanatoflavins as active-site probes for flavoproteins. Biochemistry. 30: 456-64. PMID 1670991 DOI: 10.1021/Bi00216A022 |
0.507 |
|
| 1990 |
Taylor MG, Massey V. Decay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase. The Journal of Biological Chemistry. 265: 13687-94. PMID 2380181 |
0.628 |
|
| 1990 |
Giegel DA, Williams CH, Massey V. L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family. The Journal of Biological Chemistry. 265: 6626-32. PMID 2324094 |
0.611 |
|
| 1990 |
Powlowski J, Ballou DP, Massey V. Studies of the oxidative half-reaction of anthranilate hydroxylase (deaminating) with native and modified substrates. The Journal of Biological Chemistry. 265: 4969-75. PMID 2318877 |
0.547 |
|
| 1990 |
Ludwig ML, Schopfer LM, Metzger AL, Pattridge KA, Massey V. Structure and oxidation-reduction behavior of 1-deaza-FMN flavodoxins: modulation of redox potentials in flavodoxins. Biochemistry. 29: 10364-75. PMID 2261478 DOI: 10.1021/Bi00497A011 |
0.344 |
|
| 1990 |
Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT. 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: 2831-41. PMID 2189497 DOI: 10.1021/Bi00463A028 |
0.785 |
|
| 1990 |
Fish KM, Massey V, Sands RH, Dunham WR. The interaction of bisulfite with milk xanthine oxidase. The Journal of Biological Chemistry. 265: 19665-71. PMID 2174049 |
0.303 |
|
| 1990 |
Macheroux P, Kojiro CL, Schopfer LM, Chakraborty S, Massey V. 19F NMR studies on 8-fluoroflavins and 8-fluoro flavoproteins. Biochemistry. 29: 2670-9. PMID 1971765 DOI: 10.1021/Bi00463A008 |
0.43 |
|
| 1989 |
Schopfer LM, Massey V, Ghisla S, Thorpe C. Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kinetics. Biochemistry. 27: 6599-611. PMID 3219356 DOI: 10.1021/Bi00417A059 |
0.445 |
|
| 1989 |
Einarsdottir GH, Stankovich MT, Powlowski J, Ballou DP, Massey V. Regulation of oxidation-reduction potentials of anthranilate hydroxylase from Trichosporon cutaneum by substrate and effector binding Biochemistry. 28: 4161-4168. PMID 2765477 DOI: 10.1021/Bi00436A006 |
0.675 |
|
| 1989 |
Ghisla S, Massey V. Mechanisms of flavoprotein-catalyzed reactions. European Journal of Biochemistry. 181: 1-17. PMID 2653819 DOI: 10.1111/J.1432-1033.1989.Tb14688.X |
0.395 |
|
| 1989 |
Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 28: 1194-205. PMID 2653437 DOI: 10.1021/Bi00429A037 |
0.768 |
|
| 1989 |
Brissette P, Ballou DP, Massey V. Determination of the dead time of a stopped-flow fluorometer Analytical Biochemistry. 181: 234-238. PMID 2510550 DOI: 10.1016/0003-2697(89)90235-2 |
0.528 |
|
| 1988 |
Negri A, Massey V, Williams CH, Schopfer LM. The kinetic mechanism of beef kidney D-aspartate oxidase. The Journal of Biological Chemistry. 263: 13557-63. PMID 2901415 |
0.702 |
|
| 1988 |
Manstein DJ, Massey V, Ghisla S, Pai EF. Stereochemistry and accessibility of prosthetic groups in flavoproteins Biochemistry®. 27: 2300-2305. PMID 2898258 DOI: 10.1021/Bi00407A009 |
0.483 |
|
| 1987 |
Negri A, Massey V, Williams CH. D-aspartate oxidase from beef kidney. Purification and properties. The Journal of Biological Chemistry. 262: 10026-34. PMID 3611051 |
0.681 |
|
| 1987 |
Giegel DA, Massey V, Williams CH. L-lactate-2-monooxygenase. Sequence of peptides containing residues modified by 1-fluoro-2,4-dinitrobenzene. The Journal of Biological Chemistry. 262: 5705-10. PMID 3571231 |
0.642 |
|
| 1987 |
D'Silva C, Williams CH, Massey V. Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl) hydroxylamine. Biochemistry. 26: 1717-22. PMID 2885027 DOI: 10.1021/Bi00380A034 |
0.656 |
|
| 1987 |
Massey V, Ghisla S, Yagi K. 6-Thiocyanatoflavins and 6-mercaptoflavins as active-site probes of flavoproteins. Biochemistry. 25: 8103-12. PMID 2879564 DOI: 10.1021/Bi00372A046 |
0.497 |
|
| 1987 |
Massey V, Ghisla S, Yagi K. 6-Azido- and 6-aminoflavins as active-site probes of flavin enzymes. Biochemistry. 25: 8095-102. PMID 2879563 DOI: 10.1021/Bi00372A045 |
0.485 |
|
| 1986 |
Manstein DJ, Pai EF, Schopfer LM, Massey V. Absolute stereochemistry of flavins in enzyme-catalyzed reactions Biochemistry®. 25: 6807-6816. PMID 3801393 DOI: 10.1021/Bi00370A012 |
0.474 |
|
| 1986 |
Anderson RF, Hille R, Massey V. The radical chemistry of milk xanthine oxidase as studied by radiation chemistry techniques. The Journal of Biological Chemistry. 261: 15870-6. PMID 3782094 |
0.702 |
|
| 1986 |
Hille R, Massey V. The equilibration of reducing equivalents within milk xanthine oxidase. The Journal of Biological Chemistry. 261: 1241-7. PMID 3753700 |
0.679 |
|
| 1986 |
Ghisla S, Massey V, Yagi K. Preparation and some properties of 6-substituted flavins as active site probes for flavin enzymes. Biochemistry. 25: 3282-9. PMID 3730361 DOI: 10.1021/Bi00359A030 |
0.47 |
|
| 1986 |
Miller SM, Ballou DP, Massey V, Williams CH, Walsh CT. Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction. The Journal of Biological Chemistry. 261: 8081-4. PMID 3522563 |
0.767 |
|
| 1986 |
D'Silva C, Williams CH, 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: 5602-8. PMID 2877687 DOI: 10.1021/Bi00367A039 |
0.736 |
|
| 1985 |
Gorelick RJ, Schopfer LM, Ballou DP, Massey V, Thorpe C. Interflavin oxidation - reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron-transferring flavoprotein Biochemistry. 24: 6830-6839. PMID 4074729 DOI: 10.1021/Bi00345A015 |
0.577 |
|
| 1985 |
Stewart RC, Hille R, Massey V. The reaction of arsenite-complexed xanthine oxidase with oxygen. Evidence for an oxygen-reactive molybdenum center. The Journal of Biological Chemistry. 260: 8892-904. PMID 3839506 |
0.726 |
|
| 1985 |
Fitzpatrick PF, Ghisla S, Massey V. 8-Azidoflavins as photoaffinity labels for flavoproteins. The Journal of Biological Chemistry. 260: 8483-91. PMID 2861204 |
0.575 |
|
| 1984 |
Ghisla S, Thorpe C, Massey V. Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase: Evidence for the transfer of the β-hydrogen to the flavin N(5)-position as a hydride Biochemistry. 23: 3154-3161. PMID 6466635 DOI: 10.1021/Bi00309A008 |
0.399 |
|
| 1984 |
Swenson RP, Williams CH, Massey V. Methylation of the active center histidine 217 in D-amino acid oxidase by methyl-p-nitrobenzenesulfonate. The Journal of Biological Chemistry. 259: 5585-90. PMID 6143757 |
0.806 |
|
| 1984 |
Stewart RC, Hille R, Massey V. Characterization of arsenite-complexed xanthine oxidase at room temperature. Spectral properties and pH-dependent redox behavior of the molybdenum-arsenite center. The Journal of Biological Chemistry. 259: 14426-36. PMID 6094556 |
0.7 |
|
| 1983 |
Thorpe C, Massey V. Flavin analogue studies of pig kidney general acyl-CoA dehydrogenase Biochemistry. 22: 2972-2978. PMID 6871178 DOI: 10.1021/Bi00281A029 |
0.495 |
|
| 1983 |
Zanetti G, Massey V, Curti B. FAD analogues as mechanistic and 'binding-domain' probes of spinach ferredoxin-NADP+ reductase. European Journal of Biochemistry. 132: 201-5. PMID 6840083 DOI: 10.1111/J.1432-1033.1983.Tb07348.X |
0.491 |
|
| 1983 |
Choong YS, Massey V. 2-thioriboflavin 5'-phosphate (2-thio-FMN) lactate oxidase. European Journal of Biochemistry. 131: 501-8. PMID 6840063 DOI: 10.1111/J.1432-1033.1983.Tb07290.X |
0.528 |
|
| 1983 |
Hille R, Stewart RC, Fee JA, Massey V. The interaction of arsenite with xanthine oxidase. The Journal of Biological Chemistry. 258: 4849-56. PMID 6300101 |
0.728 |
|
| 1983 |
Fitzpatrick PF, 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. The Journal of Biological Chemistry. 258: 9700-5. PMID 6136504 |
0.583 |
|
| 1983 |
Swenson RP, Williams CH, Massey V. Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride. The Journal of Biological Chemistry. 258: 497-502. PMID 6129252 |
0.793 |
|
| 1982 |
Massey V. Flavoproteins: correlation of structure and function. Advances in Experimental Medicine and Biology. 148: 295-308. PMID 7124524 DOI: 10.1007/978-1-4615-9281-5_24 |
0.371 |
|
| 1982 |
Morpeth FF, Massey V. Metal binding to D-lactate dehydrogenase. Biochemistry. 21: 1318-23. PMID 7074089 DOI: 10.1021/Bi00535A033 |
0.479 |
|
| 1982 |
Morpeth FF, Massey V. Stopped-flow kinetic studies on the D-lactate dehydrogenase from megasphera elsdenii. Biochemistry. 21: 1313-7. PMID 7074088 DOI: 10.1021/Bi00535A032 |
0.42 |
|
| 1982 |
Morpeth FF, Massey V. Steady-state kinetic studies on D-lactate dehydrogenase from Megasphera elsdenii. Biochemistry. 21: 1307-12. PMID 7074087 DOI: 10.1021/Bi00535A031 |
0.404 |
|
| 1982 |
Claiborne A, Massey V, Fitzpatrick PF, Schopfer LM. 2-Thioflavins as active site probes of flavoproteins. The Journal of Biological Chemistry. 257: 174-82. PMID 7053365 |
0.469 |
|
| 1982 |
Nishino T, Tsushima K, Hille R, Massey V. Inhibition of milk xanthine oxidase by fluorodinitrobenzene. The Journal of Biological Chemistry. 257: 7348-53. PMID 6806272 |
0.743 |
|
| 1982 |
Hille R, Massey V. The presence of a reducible disulfide bond in milk xanthine oxidase. The Journal of Biological Chemistry. 257: 8898-901. PMID 6284747 |
0.748 |
|
| 1982 |
Fitzpatrick PF, Massey V. The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics. The Journal of Biological Chemistry. 257: 12916-23. PMID 6127341 |
0.605 |
|
| 1982 |
Fitzpatrick PF, Massey V. Proton release during the reductive half-reaction of D-amino acid oxidase. The Journal of Biological Chemistry. 257: 9958-62. PMID 6125513 |
0.587 |
|
| 1982 |
Ronchi S, Minchiotti L, Galliano M, Curti B, Swenson RP, Williams CH, Massey V. The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence. The Journal of Biological Chemistry. 257: 8824-34. PMID 6124543 |
0.769 |
|
| 1982 |
Swenson RP, Williams CH, Massey V, Ronchi S, Minchiotti L, Galliano M, Curti B. The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides. The Journal of Biological Chemistry. 257: 8817-23. PMID 6124542 |
0.778 |
|
| 1982 |
Swenson RP, Williams CH, Massey V. Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. The Journal of Biological Chemistry. 257: 1937-44. PMID 6120171 |
0.803 |
|
| 1982 |
Fitzpatrick PF, Massey V. Thiazolidine-2-carboxylic acid, an adduct of cysteamine and glyoxylate, as a substrate for D-amino acid oxidase. The Journal of Biological Chemistry. 257: 1166-71. PMID 6120164 |
0.582 |
|
| 1982 |
Beinert H, Massey V. Peter Hemmerich, 1929–1981 Trends in Biochemical Sciences. 7: 43-44. DOI: 10.1016/0968-0004(82)90069-X |
0.386 |
|
| 1981 |
Hille R, Massey V. Tight binding inhibitors of xanthine oxidase. Pharmacology & Therapeutics. 14: 249-63. PMID 6895556 DOI: 10.1016/0163-7258(81)90063-2 |
0.749 |
|
| 1981 |
Hille R, Massey V. Studies on the oxidative half-reaction of xanthine oxidase. The Journal of Biological Chemistry. 256: 9090-5. PMID 6894924 |
0.736 |
|
| 1981 |
Hille R, Fee JA, Massey V. Equilibrium properties of xanthine oxidase containing FAD analogs of varying oxidation-reduction potential. The Journal of Biological Chemistry. 256: 8933-40. PMID 6894923 |
0.647 |
|
| 1980 |
Olson ST, Massey V. Reactivity of sulfhydryl groups of the flavoenzyme D-lactate dehydrogenase and effect on catalytic activity. Biochemistry. 19: 3137-44. PMID 7407035 DOI: 10.1021/Bi00555A004 |
0.346 |
|
| 1980 |
Massey V, Hemmerich P. Active-site probes of flavoproteins. Biochemical Society Transactions. 8: 246-57. PMID 7399046 DOI: 10.1042/Bst0080246 |
0.464 |
|
| 1980 |
Nishino T, Massey V. Effects of nitroaromatic compounds on spectra of D-amino acid oxidase Biochemical and Biophysical Research Communications. 95: 312-319. PMID 6106474 DOI: 10.1016/0006-291X(80)90740-8 |
0.432 |
|
| 1980 |
Nishino T, Massey V, Williams CH. Chemical modifications of D-amino acid oxidase. Evidence for active site histidine, tyrosine, and arginine residues. The Journal of Biological Chemistry. 255: 3610-6. PMID 6102567 |
0.698 |
|
| 1980 |
Ghisla S, Olson ST, Massey V, Lhoste JM. Structure of the flavin adduct formed in the suicide reaction of alpha-hydroxybutynoate with D-lactate dehydrogenase. Biochemistry. 18: 4733-42. PMID 497164 DOI: 10.1021/Bi00588A038 |
0.449 |
|
| 1980 |
Olson ST, Massey V, Ghisla S, Whitfield CD. Suicide inactivation of the flavoenzyme D-lactate dehydrogenase by alpha-hydroxybutynoate. Biochemistry. 18: 4724-32. PMID 497163 DOI: 10.1021/Bi00588A037 |
0.406 |
|
| 1980 |
Olson ST, Massey V. Purification and properties of the flavoenzyme D-lactate dehydrogenase from Megasphaera elsdenii. Biochemistry. 18: 4714-24. PMID 497162 DOI: 10.1021/Bi00588A036 |
0.495 |
|
| 1979 |
Fenner H, Grauert R, Hemmerich P, Michel H, Massey V. 5-Thia-5-deazaflavin, a 1e--transferring flavin analog. European Journal of Biochemistry / Febs. 95: 183-91. PMID 222578 DOI: 10.1111/J.1432-1033.1979.Tb12952.X |
0.369 |
|
| 1979 |
Massey V, Mendelsohn LD. Immobilized glucose oxidase and D-amino acid oxidase: a convenient method for the purification of flavin adenine dinucleotide and its analogs. Analytical Biochemistry. 95: 156-9. PMID 40451 DOI: 10.1016/0003-2697(79)90198-2 |
0.405 |
|
| 1979 |
Husain M, Schopfer LM, Massey V. P-Hydroxybenzoate hydroxylase and melilotate hydroxylase. Methods in Enzymology. 53: 543-58. PMID 30879 DOI: 10.1016/S0076-6879(78)53056-5 |
0.413 |
|
| 1978 |
Massey V, Hemmerich P. Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Biochemistry. 17: 9-16. PMID 618550 DOI: 10.1021/Bi00594A002 |
0.332 |
|
| 1978 |
Massey V, Stankovich M, Hemmerich P. Light-mediated reduction of flavoproteins with flavins as catalysts. Biochemistry. 17: 1-8. PMID 618535 DOI: 10.1021/Bi00594A001 |
0.427 |
|
| 1978 |
Husain M, Massey V. [44] Reversible resolution of flavoproteins into apoproteins and free flavins Methods in Enzymology. 53: 429-437. DOI: 10.1016/S0076-6879(78)53047-4 |
0.385 |
|
| 1977 |
Quay S, Massey V. Effect of pH on the interaction of benzoate and D-amino acid oxidase. Biochemistry. 16: 3348-54. PMID 19047 DOI: 10.1021/Bi00634A010 |
0.465 |
|
| 1977 |
Ghisla S, Entsch B, Massey V, Husein M. On the structure of flavin-oxygen intermediates involved in enzymatic reactions. European Journal of Biochemistry. 76: 139-48. PMID 18348 DOI: 10.1111/J.1432-1033.1977.Tb11579.X |
0.448 |
|
| 1976 |
Schonbrunn A, Abeles RH, Walsh CT, Ghisla S, Ogata H, Massey V. The structure of the covalent flavin adduct formed between lactate oxidase and the suicide substrate 2-hydroxy-3-butynoate. Biochemistry. 15: 1798-807. PMID 1268196 DOI: 10.1021/Bi00654A003 |
0.447 |
|
| 1976 |
Ghisla S, Ogata H, Massey V, Schonbrunn A, Abeles RH, Walsh CT. Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate] 2-hydroxy-3-butynoate. Biochemistry. 15: 1791-7. PMID 1268195 DOI: 10.1021/Bi00654A002 |
0.492 |
|
| 1975 |
Matthews RG, Massey V, Sweeley CC. Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. The Journal of Biological Chemistry. 250: 9294-8. PMID 1194284 |
0.709 |
|
| 1975 |
Strickland S, Schopfer LM, Massey V. Kinetic and mechanistic studies on the reaction of melilotate hydroxylase with deuterated melilotate Biochemistry. 14: 2230-2235. PMID 1148167 DOI: 10.1021/Bi00681A029 |
0.45 |
|
| 1975 |
Strickland S, Palmer G, Massey V. Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. The Journal of Biological Chemistry. 250: 4048-52. PMID 1126943 |
0.544 |
|
| 1974 |
Entsch B, Massey V, Ballou DP. Intermediates in flavoprotein catalyzed hydroxylations. Biochemical and Biophysical Research Communications. 57: 1018-25. PMID 4830743 DOI: 10.1016/0006-291X(74)90798-0 |
0.633 |
|
| 1974 |
Olson JS, Ballou DP, Palmer G, Massey V. The mechanism of action of xanthine oxidase. The Journal of Biological Chemistry. 249: 4363-82. PMID 4367215 |
0.719 |
|
| 1974 |
Olson JS, Ballow DP, Palmer G, Massey V. The reaction of xanthine oxidase with molecular oxygen. The Journal of Biological Chemistry. 249: 4350-62. PMID 4367214 |
0.69 |
|
| 1974 |
Massey V, Ghisla S. ROLE OF CHARGE-TRANSFER INTERACTIONS IN FLAVOPROTEIN CATALYSIS Annals of the New York Academy of Sciences. 227: 446-465. DOI: 10.1111/J.1749-6632.1974.Tb14407.X |
0.399 |
|
| 1973 |
Mayhew SG, Massey V. Studies on the kinetics and mechanism of reduction of flavodoxin from Peptostreptococcus elsdenii by sodium dithionite. Biochimica Et Biophysica Acta. 315: 181-90. PMID 4743900 DOI: 10.1016/0005-2744(73)90141-1 |
0.37 |
|
| 1973 |
Edmondson D, Ballou D, Van Heuvelen A, Palmer G, Massey V. Kinetic studies on the substrate reduction of xanthine oxidase. The Journal of Biological Chemistry. 248: 6135-44. PMID 4353632 |
0.554 |
|
| 1972 |
Tanaka M, Haniu M, Matsueda G, Yasunobu KT, Mayhew S, Massey V. Amino- and carboxyl-terminal amino acid sequences of the Peptostreptococcus eisdenii and Clostridium pasteurianum flavodoxins. Biochemistry. 10: 3041-6. PMID 5126921 DOI: 10.1021/Bi00792A009 |
0.302 |
|
| 1972 |
Tanaka M, Haniu M, Yasunobu KT, Mayhew S, Massey V. Amino acid sequence of the Peptostreptococcus elsdenii flavodoxin. Biochemical and Biophysical Research Communications. 44: 886-92. PMID 5125231 DOI: 10.1016/0006-291X(71)90794-7 |
0.358 |
|
| 1972 |
Massey V, Edmondson D, Palmer G, Beacham LM, Elion GB. The separation of functional and non-functional xanthine oxidase by affinity chromatography. The Biochemical Journal. 127: 10P-11P. PMID 4672853 DOI: 10.1042/Bj1270010P |
0.465 |
|
| 1972 |
Spector T, Massey V. Interactions of substrate and non-substrate effectors with p-hydroxybenzoate hydroxylase from pseudomonas fluorescens. Biochemical and Biophysical Research Communications. 45: 1219-26. PMID 4400084 DOI: 10.1016/0006-291X(71)90148-3 |
0.459 |
|
| 1972 |
Müller F, Brüstlein M, Hemmerich P, Massey V, Walker WH. Light-absorption studies on neutral flavin radicals. European Journal of Biochemistry / Febs. 25: 573-80. PMID 4339644 DOI: 10.1111/J.1432-1033.1972.Tb01730.X |
0.301 |
|
| 1972 |
Edmondson D, Massey V, Palmer G, Beacham LM, Elion GB. The resolution of active and inactive xanthine oxidase by affinity chromatography. The Journal of Biological Chemistry. 247: 1597-604. PMID 4335003 |
0.453 |
|
| 1971 |
Schuman M, Massey V. Effect of anions on the catalytic activity of pig liver glycolic acid oxidase Bba - Enzymology. 227: 521-537. PMID 5569123 DOI: 10.1016/0005-2744(71)90004-0 |
0.464 |
|
| 1971 |
Schuman M, Massey V. Purification and characterization of glycolic acid oxidase from pig liver Bba - Enzymology. 227: 500-520. PMID 5569122 DOI: 10.1016/0005-2744(71)90003-9 |
0.449 |
|
| 1971 |
Massey V, Williams CH, Palmer G. The presence of S degrees-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c. Biochemical and Biophysical Research Communications. 42: 730-8. PMID 5543955 DOI: 10.1016/0006-291X(71)90548-1 |
0.703 |
|
| 1971 |
Zimmerman SE, Brown RK, Curti B, Massey V. Immunochemical studies of L-amino acid oxidase. Biochimica Et Biophysica Acta. 229: 260-70. PMID 5543611 DOI: 10.1016/0005-2795(71)90341-2 |
0.416 |
|
| 1971 |
Mayhew SG, Massey V. Evidence for a novel flavin prosthetic group associated with NADH dehydrogenase from Peptostreptococcus elsdenii. Biochimica Et Biophysica Acta. 235: 303-310. PMID 5317636 DOI: 10.1016/0005-2744(71)90208-7 |
0.314 |
|
| 1971 |
Engel PC, Massey V. Green butyryl-coenzyme A dehydrogenase. An enzyme-acyl-coenzyme A complex Biochemical Journal. 125: 889-902. PMID 5145911 DOI: 10.1042/Bj1250889 |
0.645 |
|
| 1971 |
Engel PC, Massey V. The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii Biochemical Journal. 125: 879-887. PMID 5145910 DOI: 10.1042/Bj1250879 |
0.629 |
|
| 1971 |
Howell LG, Massey V. A non-substrate effector of p-hydroxybenzoate hydroxylase. Biochemical and Biophysical Research Communications. 40: 887-93. PMID 4395604 DOI: 10.1016/0006-291X(70)90986-1 |
0.436 |
|
| 1971 |
Müller F, Massey V, Hemmerich P. [151] On the reduction of d- and l-amino acid oxidases and free flavins by borohydride yielding 3,4-dihydroflavin analogs Methods in Enzymology. 18: 474-479. DOI: 10.1016/S0076-6879(71)18108-6 |
0.514 |
|
| 1971 |
Müller F, Massey V. [150] Sulfite interaction with free and protein-bound flavin: Flavin + SO32− ⇌flavin-SO3−complex Methods in Enzymology. 18: 468-473. DOI: 10.1016/S0076-6879(71)18107-4 |
0.313 |
|
| 1970 |
Massey V, Komai H, Palmer G, Elion GB. On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines. The Journal of Biological Chemistry. 245: 2837-44. PMID 5467924 |
0.452 |
|
| 1970 |
Walker WH, Hemmerich P, Massey V. Light-induced alkylation and dealkylation of the flavin nucleus. Stable dihydroflavins: spectral course and mechanism of formation European Journal of Biochemistry. 13: 258-266. PMID 5439931 DOI: 10.1111/J.1432-1033.1970.Tb00926.X |
0.354 |
|
| 1970 |
Massey V, Komai H, Palmer G, Elion GB. The existence of nonfunctional active sites in milk xanthine oxidase: reaction with functional active site inhibitors. Vitamins and Hormones. 28: 505-31. PMID 4335890 DOI: 10.1016/S0083-6729(08)60909-7 |
0.522 |
|
| 1970 |
Müller F, Hemmerich P, Ehrenberg A, Palmer G, 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. European Journal of Biochemistry / Febs. 14: 185-96. PMID 4315843 DOI: 10.1111/J.1432-1033.1970.Tb00277.X |
0.486 |
|
| 1969 |
Foust GP, Burleigh BD, Mayhew SG, Williams CH, Massey V. An anaerobic titration assembly for spectrophotometric use. Analytical Biochemistry. 27: 530-5. PMID 5767206 DOI: 10.1016/0003-2697(69)90066-9 |
0.574 |
|
| 1969 |
Massey V, Strickland S, Mayhew SG, Howell LG, Engel PC, Matthews RG, Schuman M, Sullivan PA. The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen. Biochemical and Biophysical Research Communications. 36: 891-7. PMID 5388670 DOI: 10.1016/0006-291X(69)90287-3 |
0.79 |
|
| 1969 |
Massey V, Müller F, Feldberg R, Schuman M, Sullivan PA, Howell LG, Mayhew SG, Matthews RG, Foust GP. The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity. The Journal of Biological Chemistry. 244: 3999-4006. PMID 4389773 |
0.632 |
|
| 1969 |
Matthews RG, Massey V. Isolation of old yellow enzyme in free and complexed forms. The Journal of Biological Chemistry. 244: 1779-86. PMID 4388613 |
0.689 |
|
| 1969 |
Ballou D, Palmer G, Massey V. Direct demonstration of superoxide anion production during the oxidation of reduced flavin and of its catalytic decomposition by erythrocuprein. Biochemical and Biophysical Research Communications. 36: 898-904. PMID 4310146 DOI: 10.1016/0006-291X(69)90288-5 |
0.682 |
|
| 1969 |
Müller F, Massey V, Heizmann C, Hemmerich P, Lhoste JM, Gould DC. The reduction of flavins by borohydride: 3,4-dihydroflavin. Struction, absorption and luminescence. European Journal of Biochemistry / Febs. 9: 392-401. PMID 4307593 DOI: 10.1111/J.1432-1033.1969.Tb00621.X |
0.385 |
|
| 1969 |
Palmer G, Massey V. Electron paramagnetic resonance and circular dichroism studies on milk xanthine oxidase. The Journal of Biological Chemistry. 244: 2614-20. PMID 4306032 |
0.4 |
|
| 1969 |
Komai H, Massey V, Palmer G. The preparation and properties of deflavo xanthine oxidase. The Journal of Biological Chemistry. 244: 1692-700. PMID 4305460 |
0.427 |
|
| 1968 |
Zanetti G, Williams CH, Massey V. Influence of photoirradiation on the oxidation-reduction state of thioredoxin reductase. The Journal of Biological Chemistry. 243: 4013-9. PMID 4299099 |
0.578 |
|
| 1967 |
Hemmerich P, Massey V, Weber G. Photo-induced benzyl substitution of flavins by phenylacetate: A possible model for flavoprotein catalysis [38] Nature. 213: 728-730. DOI: 10.1038/213728A0 |
0.488 |
|
| 1966 |
Massey V, Palmer G. On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry. 5: 3181-9. PMID 4382016 DOI: 10.1021/Bi00874A016 |
0.449 |
|
| 1966 |
Massey V, Ganther H. On the interpretation of the absorption spectra of flavoproteins with special reference to D-amino acid oxidase. Biochemistry. 4: 1161-73. PMID 4378783 DOI: 10.1021/Bi00882A027 |
0.311 |
|
| 1965 |
Massey V, Williams CH. On the reaction mechanism of yeast glutathione reductase. The Journal of Biological Chemistry. 240: 4470-80. PMID 4378936 |
0.616 |
|
| 1962 |
PALMER G, MASSEY V. On the sulphydryl groups of lipoamide dehydrogenase. Biochimica Et Biophysica Acta. 58: 349-50. PMID 14483404 DOI: 10.1016/0006-3002(62)91019-3 |
0.468 |
|
| 1962 |
MASSEY V, PALMER G. Charge transfer complexes of lipoyl dehydrogenase and free flavins. The Journal of Biological Chemistry. 237: 2347-58. PMID 14470919 |
0.428 |
|
| 1962 |
MASSEY V, HOFMANN T, PALMER G. The relation of function and structure in lipoyl dehydrogenase. The Journal of Biological Chemistry. 237: 3820-8. PMID 13933422 |
0.397 |
|
| 1961 |
MASSEY V, PALMER G, BENNETT R. The purification and some properties of D-amino acid oxidase. Biochimica Et Biophysica Acta. 48: 1-9. PMID 13767909 |
0.469 |
|
| 1956 |
HARTLEY BS, MASSEY V. The active centre of chymotrypsin. II. Reaction with fluorodinitrobenzene. Biochimica Et Biophysica Acta. 21: 361-7. PMID 13363919 DOI: 10.1016/0006-3002(56)90020-8 |
0.556 |
|
| 1956 |
HARTLEY BS, MASSEY V. The active centre of chymotrypsin. I. Labelling with a fluorescent dye. Biochimica Et Biophysica Acta. 21: 58-70. PMID 13363860 DOI: 10.1016/0006-3002(56)90093-2 |
0.507 |
|
| 1956 |
SINGER TP, MASSEY V, KEARNEY EB. On the reversibility of succinic dehydrogenase. Biochimica Et Biophysica Acta. 19: 200-1. PMID 13304101 DOI: 10.1016/0006-3002(56)90417-6 |
0.385 |
|
| 1956 |
SINGER TP, KEARNEY EB, MASSEY V. Observations on the flavin moiety of succinic dehydrogenase. Archives of Biochemistry and Biophysics. 60: 255-7. PMID 13283607 DOI: 10.1016/0003-9861(56)90415-5 |
0.415 |
|
| 1954 |
MASSEY V, ALBERTY RA. Ionisation constants of fumarase. Biochimica Et Biophysica Acta. 13: 354-9. PMID 13140347 |
0.44 |
|
| 1954 |
ALBERTY RA, MASSEY V. On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction. Biochimica Et Biophysica Acta. 13: 347-53. PMID 13140346 |
0.563 |
|
| 1954 |
Alberty RA, Massey V, Frieden C, Fuhlbrigge AR. Studies of the Enzyme Fumarase. III.1The Dependence of the Kinetic Constants at 25° upon the Concentration and pH of Phosphate Buffers Journal of the American Chemical Society. 76: 2485-2493. DOI: 10.1021/Ja01638A053 |
0.695 |
|
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