| Year |
Citation |
Score |
| 2023 |
Roman JV, Mascarenhas R, Ceric K, Ballou DP, Banerjee R. Disease-causing cystathionine β-synthase linker mutations impair allosteric regulation. The Journal of Biological Chemistry. 105449. PMID 37949228 DOI: 10.1016/j.jbc.2023.105449 |
0.31 |
|
| 2022 |
Collins DP, Johnson E, Coulter ED, Beharry Z, Ballou DP, Dawson JH. Caught in the act: Monitoring OO bond cleavage in Acylperoxoferric cytochrome P450cam to form compound I in real time. Journal of Inorganic Biochemistry. 111949. PMID 36028338 DOI: 10.1016/j.jinorgbio.2022.111949 |
0.323 |
|
| 2020 |
Kaneshiro AK, Koebke KJ, Zhao C, Ferguson KL, Ballou DP, Palfey BA, Ruotolo BT, Marsh ENG. Kinetic Analysis of Transient Intermediates in the Mechanism of Prenyl-Flavin-Dependent Ferulic Acid Decarboxylase. Biochemistry. PMID 33342208 DOI: 10.1021/acs.biochem.0c00856 |
0.42 |
|
| 2020 |
Tinikul R, Lawan N, Akeratchatapan N, Pimviriyakul P, Chinantuya W, Suadee C, Sucharitakul J, Chenprakhon P, Ballou DP, Entsch B, Chaiyen P. Protonation Status and Control Mechanism of Flavin-Oxygen Intermediates in the Reaction of Bacterial Luciferase. The Febs Journal. PMID 33289305 DOI: 10.1111/febs.15653 |
0.589 |
|
| 2018 |
Landry AP, Ballou DP, Banerjee R. Modulation of catalytic promiscuity during hydrogen sulfide oxidation. Acs Chemical Biology. PMID 29715001 DOI: 10.1021/Acschembio.8B00258 |
0.451 |
|
| 2018 |
Hazra AB, Ballou DP, Taga ME. Unique biochemical and sequence features enable BluB to destroy flavin and distinguish BluB from the flavin monooxygenase superfamily. Biochemistry. PMID 29457884 DOI: 10.1021/Acs.Biochem.7B01193 |
0.487 |
|
| 2018 |
Zuo C, Jolly AL, Nikolova AP, Satzer DI, Cao S, Sanchez JS, Ballou DP, Trimmer EE. A role for glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli. Archives of Biochemistry and Biophysics. PMID 29407039 DOI: 10.1016/J.Abb.2018.01.014 |
0.521 |
|
| 2017 |
Landry AP, Ballou DP, Banerjee R. H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase. The Journal of Biological Chemistry. PMID 28512131 DOI: 10.1074/Jbc.M117.788547 |
0.424 |
|
| 2016 |
Catucci G, Zgrablic I, Lanciani F, Valetti F, Minerdi D, Ballou DP, Gilardi G, Sadeghi SJ. Characterization of a new Baeyer-Villiger monooxygenase and conversion to a solely N-or S-oxidizing enzyme by a single R292 mutation. Biochimica Et Biophysica Acta. PMID 27344049 DOI: 10.1016/J.Bbapap.2016.06.010 |
0.339 |
|
| 2016 |
Spolitak T, Hollenberg PF, Ballou DP. Oxidative hemoglobin reactions: Applications to drug metabolism. Archives of Biochemistry and Biophysics. PMID 27091316 DOI: 10.1016/J.Abb.2016.04.007 |
0.638 |
|
| 2016 |
Carballal S, Cuevasanta E, Yadav PK, Gherasim C, Ballou DP, Alvarez B, Banerjee R. Kinetics of nitrite reduction and peroxynitrite formation by ferrous heme in human cystathionine β-synthase. The Journal of Biological Chemistry. PMID 26867575 DOI: 10.1074/Jbc.M116.718734 |
0.368 |
|
| 2016 |
Gao Y, Dai X, Zheng Z, Kasahara H, Kamiya Y, Chory J, Ballou D, Zhao Y. Overexpression of the bacterial tryptophan oxidase RebO affects auxin biosynthesis and Arabidopsis development Science Bulletin. 1-9. DOI: 10.1007/S11434-016-1066-2 |
0.332 |
|
| 2015 |
Carballal S, Cuevasanta E, Marmisolle I, Kabil O, Gherasim C, Ballou DP, Banerjee R, Alvarez B. Correction to Kinetics of Reversible Reductive Carbonylation of Heme in Human Cystathionine β-Synthase. Biochemistry. PMID 26710076 DOI: 10.1021/Acs.Biochem.5B01326 |
0.332 |
|
| 2015 |
Mishanina TV, Yadav PK, Ballou DP, Banerjee R. Transient Kinetic Analysis of Hydrogen Sulfide Oxidation Catalyzed by Human Sulfide Quinone Oxidoreductase. The Journal of Biological Chemistry. 290: 25072-80. PMID 26318450 DOI: 10.1074/Jbc.M115.682369 |
0.48 |
|
| 2015 |
Bobyk KD, Ballou DP, Rokita SE. Rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid. Biochemistry. 54: 4487-94. PMID 26151430 DOI: 10.1021/Acs.Biochem.5B00410 |
0.488 |
|
| 2015 |
Spolitak T, Ballou DP. Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD Archives of Biochemistry and Biophysics. 573: 111-119. PMID 25837855 DOI: 10.1016/J.Abb.2015.03.020 |
0.458 |
|
| 2015 |
Carballal S, Gherasim C, Yadav PK, Cuevasanta E, Ballou DP, Alvarez B, Banerjee R. 272 - Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine P-Synthase Free Radical Biology and Medicine. 87. DOI: 10.1016/J.Freeradbiomed.2015.10.320 |
0.415 |
|
| 2013 |
Tinikul R, Pitsawong W, Sucharitakul J, Nijvipakul S, Ballou DP, Chaiyen P. The transfer of reduced flavin mononucleotide from luxg oxidoreductase to luciferase occurs via free diffusion Biochemistry. 52: 6834-6843. PMID 24004065 DOI: 10.1021/Bi4006545 |
0.685 |
|
| 2013 |
Dai X, Mashiguchi K, Chen Q, Kasahara H, Kamiya Y, Ojha S, DuBois J, Ballou D, Zhao Y. The biochemical mechanism of auxin biosynthesis by an arabidopsis YUCCA flavin-containing monooxygenase. The Journal of Biological Chemistry. 288: 1448-57. PMID 23188833 DOI: 10.1074/Jbc.M112.424077 |
0.48 |
|
| 2013 |
Collins DP, Isaac IS, Coulter ED, Hager PW, Ballou DP, Dawson JH. Reaction of ferric Caldariomyces fumago chloroperoxidase with meta-chloroperoxybenzoic acid: Journal of Porphyrins and Phthalocyanines. 17: 63-72. DOI: 10.1142/S1088424612501234 |
0.435 |
|
| 2012 |
Phongsak T, Sucharitakul J, Thotsaporn K, Oonanant W, Yuvaniyama J, Svasti J, Ballou DP, Chaiyen P. The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain Journal of Biological Chemistry. 287: 26213-26222. PMID 22661720 DOI: 10.1074/Jbc.M112.354472 |
0.644 |
|
| 2012 |
De Matteis F, Ballou DP, Coon MJ, Estabrook RW, Haines DC. Peroxidase-like activity of uncoupled cytochrome P450: studies with bilirubin and toxicological implications of uncoupling. Biochemical Pharmacology. 84: 374-82. PMID 22564776 DOI: 10.1016/J.Bcp.2012.04.016 |
0.623 |
|
| 2012 |
Carballa S, Cuevasanta E, Marmisolle I, Kabil O, Gherasim C, Ballou DP, Graña M, Banerjee R, Alvare B. The Heme in Human Cystathionine ?-Synthase: Kinetics of Reduction and Reoxidation Free Radical Biology and Medicine. 53: S146. DOI: 10.1016/J.Freeradbiomed.2012.10.393 |
0.344 |
|
| 2011 |
Cheng Z, Zhang J, Ballou DP, Williams CH. Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase. Chemical Reviews. 111: 5768-83. PMID 21793530 DOI: 10.1021/Cr100006X |
0.483 |
|
| 2011 |
Zhang H, Sridar C, Kenaan C, Amunugama H, Ballou DP, Hollenberg PF. Polymorphic variants of cytochrome P450 2B6 (CYP2B6.4-CYP2B6.9) exhibit altered rates of metabolism for bupropion and efavirenz: A charge-reversal mutation in the K139E variant (CYP2B6.8) impairs formation of a functional cytochrome P450-reductase complex Journal of Pharmacology and Experimental Therapeutics. 338: 803-809. PMID 21659470 DOI: 10.1124/Jpet.111.183111 |
0.644 |
|
| 2011 |
Huang HH, Day L, Cass CL, Ballou DP, Williams CH, Williams DL. Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni. Biochemistry. 50: 5870-82. PMID 21630672 DOI: 10.1021/Bi200107N |
0.621 |
|
| 2011 |
Galinato MG, Spolitak T, Ballou DP, Lehnert N. Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy. Biochemistry. 50: 1053-69. PMID 21158478 DOI: 10.1021/Bi101911Y |
0.32 |
|
| 2011 |
Singh S, Ballou DP, Banerjee R. Pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine β-synthase-catalyzed H2S generation Biochemistry. 50: 419-425. PMID 21141970 DOI: 10.1021/Bi1010893 |
0.413 |
|
| 2010 |
Nijvipakul S, Ballou DP, Chaiyen P. Reduction kinetics of a flavin oxidoreductase LuxG from photobacterium leiognathi (TH1): Half-sites reactivity Biochemistry. 49: 9241-9248. PMID 20836540 DOI: 10.1021/Bi1009985 |
0.644 |
|
| 2010 |
Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL. Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. The Journal of Biological Chemistry. 285: 30375-88. PMID 20650894 DOI: 10.1074/Jbc.M110.157578 |
0.459 |
|
| 2010 |
Chakraborty S, Ortiz-Maldonado M, Entsch B, Ballou DP. Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: A system composed of a small flavin reductase and a large flavin-dependent oxygenase Biochemistry. 49: 372-385. PMID 20000468 DOI: 10.1021/Bi901454U |
0.838 |
|
| 2010 |
Spolitak T, Funhoff EG, Ballou DP. Spectroscopic studies of the oxidation of ferric CYP153A6 by peracids: Insights into P450 higher oxidation states Archives of Biochemistry and Biophysics. 493: 184-191. PMID 19879854 DOI: 10.1016/J.Abb.2009.10.014 |
0.451 |
|
| 2009 |
Lee MN, Takawira D, Nikolova AP, Ballou DP, Furtado VC, Phung NL, Still BR, Thorstad MK, Tanner JJ, Trimmer EE. Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli. Biochemistry. 48: 7673-85. PMID 19610625 DOI: 10.1021/Bi9007325 |
0.478 |
|
| 2009 |
Tarasev M, Pullela S, Ballou DP. Distal end of 105-125 loop - A putative reductase binding domain of phthalate dioxygenase Archives of Biochemistry and Biophysics. 487: 10-18. PMID 19464996 DOI: 10.1016/J.Abb.2009.05.008 |
0.422 |
|
| 2009 |
Shebley M, Kent UM, Ballou DP, Hollenberg PF. Mechanistic analysis of the inactivation of cytochrome P450 2B6 by phencyclidine: Effects on substrate binding, electron transfer, and uncoupling Drug Metabolism and Disposition. 37: 745-752. PMID 19144770 DOI: 10.1124/Dmd.108.024661 |
0.651 |
|
| 2008 |
Ryan KS, Chakraborty S, Howard-Jones AR, Walsh CT, Ballou DP, Drennan CL. The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction. Biochemistry. 47: 13506-13. PMID 19035832 DOI: 10.1021/Bi801229W |
0.474 |
|
| 2008 |
Huang HH, Arscott LD, Ballou DP, Williams CH. Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster. Biochemistry. 47: 12769-76. PMID 18991392 DOI: 10.1021/Bi801449H |
0.657 |
|
| 2008 |
Spolitak T, Dawson JH, Ballou DP. Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 599-611. PMID 18273651 DOI: 10.1007/S00775-008-0348-9 |
0.406 |
|
| 2008 |
Padovani D, Labunska T, Palfey BA, Ballou DP, Banerjee R. Adenosyltransferase tailors and delivers coenzyme B12 Nature Chemical Biology. 4: 194-196. PMID 18264093 DOI: 10.1038/Nchembio.67 |
0.463 |
|
| 2008 |
Valton J, Mathevon C, Fontecave M, Nivière V, Ballou DP. Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor Journal of Biological Chemistry. 283: 10287-10296. PMID 18245777 DOI: 10.1074/Jbc.M709730200 |
0.477 |
|
| 2008 |
Huang HH, Arscott LD, Ballou DP, Williams CH. Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster. Biochemistry. 47: 1721-31. PMID 18211101 DOI: 10.1021/Bi702040U |
0.648 |
|
| 2008 |
Alexander JP, Ryan TJ, Ballou DP, Coward JK. Gamma-glutamyl hydrolase: kinetic characterization of isopeptide hydrolysis using fluorogenic substrates. Biochemistry. 47: 1228-39. PMID 18171026 DOI: 10.1021/Bi701607V |
0.448 |
|
| 2008 |
Nijvipakul S, Wongratana J, Suadee C, Entsch B, Ballou DP, Chaiyen P. LuxG is a functioning flavin reductase for bacterial luminescence Journal of Bacteriology. 190: 1531-1538. PMID 18156264 DOI: 10.1128/Jb.01660-07 |
0.698 |
|
| 2007 |
Ballou DP. Crystallography gets the jump on the enzymologists Proceedings of the National Academy of Sciences of the United States of America. 104: 15587-15588. PMID 17898164 DOI: 10.1073/Pnas.0707843104 |
0.436 |
|
| 2007 |
Suadee C, Nijvipakul S, Svasti J, Entsch B, Ballou DP, Chaiyen P. Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologues Journal of Biochemistry. 142: 539-552. PMID 17761697 DOI: 10.1093/Jb/Mvm155 |
0.674 |
|
| 2007 |
Sucharitakul J, Phongsak T, Entsch B, Svasti J, Chaiyen P, Ballou DP. Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase Biochemistry. 46: 8611-8623. PMID 17595116 DOI: 10.1021/Bi7006614 |
0.621 |
|
| 2007 |
Cheng Z, Arscott LD, Ballou DP, Williams CH. The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila. Biochemistry. 46: 7875-85. PMID 17550271 DOI: 10.1021/Bi700442R |
0.474 |
|
| 2007 |
Tapley TL, Eichner T, Gleiter S, Ballou DP, Bardwell JCA. Kinetic characterization of the disulfide bond-forming enzyme DsbB Journal of Biological Chemistry. 282: 10263-10271. PMID 17267399 DOI: 10.1074/Jbc.M611541200 |
0.429 |
|
| 2006 |
Spolitak T, Dawson JH, Ballou DP. Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES. Journal of Inorganic Biochemistry. 100: 2034-44. PMID 17095096 DOI: 10.1016/J.Jinorgbio.2006.09.026 |
0.452 |
|
| 2006 |
Raner GM, Thompson JI, Haddy A, Tangham V, Bynum N, Ramachandra Reddy G, Ballou DP, Dawson JH. Spectroscopic investigations of intermediates in the reaction of cytochrome P450(BM3)-F87G with surrogate oxygen atom donors. Journal of Inorganic Biochemistry. 100: 2045-53. PMID 17083977 DOI: 10.1016/J.Jinorgbio.2006.09.025 |
0.484 |
|
| 2006 |
McMillan PJ, Arscott LD, Ballou DP, Becker K, Williams CH, Müller S. Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum. The Journal of Biological Chemistry. 281: 32967-77. PMID 16950793 DOI: 10.1074/Jbc.M601141200 |
0.489 |
|
| 2006 |
Tarasev M, Pinto A, Kim D, Elliott SJ, Ballou DP. The "bridging" aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron(II)-mononuclear center Biochemistry. 45: 10208-10216. PMID 16922496 DOI: 10.1021/Bi060219B |
0.385 |
|
| 2006 |
Pinto A, Tarasev M, Ballou DP. Substitutions of the "bridging" aspartate 178 result in profound changes in the reactivity of the Rieske center of phthalate dioxygenase Biochemistry. 45: 9032-9041. PMID 16866348 DOI: 10.1021/Bi060216Z |
0.428 |
|
| 2006 |
Johansson L, Arscott LD, Ballou DP, Williams CH, Arnér ES. Studies of an active site mutant of the selenoprotein thioredoxin reductase: the Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme. Free Radical Biology & Medicine. 41: 649-56. PMID 16863998 DOI: 10.1016/J.Freeradbiomed.2006.05.005 |
0.48 |
|
| 2006 |
Yeh E, Cole LJ, Barr EW, Bollinger JM, Ballou DP, Walsh CT. Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH. Biochemistry. 45: 7904-12. PMID 16784243 DOI: 10.1021/Bi060607D |
0.478 |
|
| 2006 |
Sucharitakul J, Chaiyen P, Entsch B, Ballou DP. Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii Journal of Biological Chemistry. 281: 17044-17053. PMID 16627482 DOI: 10.1074/Jbc.M512385200 |
0.625 |
|
| 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 |
0.627 |
|
| 2005 |
Cole LJ, Entsch B, Ortiz-Maldonado M, Ballou DP. Properties of p-Hydroxybenzoate hydroxylase when stabilized in its Open conformation Biochemistry. 44: 14807-14817. PMID 16274228 DOI: 10.1021/Bi0512142 |
0.849 |
|
| 2005 |
Ballou DP, Entsch B, Cole LJ. Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases Biochemical and Biophysical Research Communications. 338: 590-598. PMID 16236251 DOI: 10.1016/J.Bbrc.2005.09.081 |
0.544 |
|
| 2005 |
Glascock MC, Ballou DP, Dawson JH. Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P-450-CAM: probing the effector role of putidaredoxin in catalysis. The Journal of Biological Chemistry. 280: 42134-41. PMID 16115886 DOI: 10.1074/Jbc.M505426200 |
0.516 |
|
| 2005 |
Sucharitakul J, Chaiyen P, Entsch B, Ballou DP. The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis Biochemistry. 44: 10434-10442. PMID 16042421 DOI: 10.1021/Bi050615E |
0.62 |
|
| 2005 |
Cole LJ, Gatti DL, Entsch B, Ballou DP. Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase Biochemistry. 44: 8047-8058. PMID 15924424 DOI: 10.1021/Bi050108X |
0.513 |
|
| 2005 |
Trimmer EE, Ballou DP, Galloway LJ, Scannell SA, Brinker DR, Casas KR. Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase: Evidence for major roles in folate binding and catalysis and a minor role in flavin reactivity Biochemistry. 44: 6809-6822. PMID 15865426 DOI: 10.1021/Bi0477236 |
0.494 |
|
| 2005 |
Tarasev M, Ballou DP. Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase Biochemistry. 44: 6197-6207. PMID 15835907 DOI: 10.1021/Bi047724Y |
0.411 |
|
| 2005 |
Deponte M, Urig S, Arscott LD, Fritz-Wolf K, Réau R, Herold-Mende C, Koncarevic S, Meyer M, Davioud-Charvet E, Ballou DP, Williams CH, Becker K. Mechanistic studies on a novel, highly potent gold-phosphole inhibitor of human glutathione reductase. The Journal of Biological Chemistry. 280: 20628-37. PMID 15792952 DOI: 10.1074/Jbc.M412519200 |
0.404 |
|
| 2005 |
Spolitak T, Dawson JH, Ballou DP. Reaction of ferric cytochrome P450cam with peracids: kinetic characterization of intermediates on the reaction pathway. The Journal of Biological Chemistry. 280: 20300-9. PMID 15781454 DOI: 10.1074/Jbc.M501761200 |
0.413 |
|
| 2005 |
Grzyska PK, Ryle MJ, Monterosso GR, Liu J, Ballou DP, Hausinger RP. Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediate. Biochemistry. 44: 3845-55. PMID 15751960 DOI: 10.1021/Bi048746N |
0.427 |
|
| 2005 |
Entsch B, Cole LJ, Ballou DP. Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase Archives of Biochemistry and Biophysics. 433: 297-311. PMID 15581585 DOI: 10.1016/J.Abb.2004.09.029 |
0.558 |
|
| 2004 |
Ortiz-Maldonado M, Entsch B, Ballou DP. Oxygen reactions in p-Hydroxybenzoate hydroxylase utilize the H-bond network during catalysis Biochemistry. 43: 15246-15257. PMID 15568817 DOI: 10.1021/Bi048115T |
0.838 |
|
| 2004 |
Tarasev M, Rhames F, Ballou DP. Rates of the phthalate dioxygenase reaction with oxygen are dramatically increased by interactions with phthalate and phthalate oxygenase reductase Biochemistry. 43: 12799-12808. PMID 15461452 DOI: 10.1021/Bi0490587 |
0.392 |
|
| 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 |
0.776 |
|
| 2004 |
Xia L, Ballou DP, Marsh ENG. Role of Arg100 in the Active Site of Adenosylcobalamin-Dependent Glutamate Mutase Biochemistry. 43: 3238-3245. PMID 15023074 DOI: 10.1021/Bi0357558 |
0.454 |
|
| 2004 |
Kent UM, Pascual L, Roof RA, Ballou DP, Hollenberg PF. Mechanistic studies with N-benzyl-1-aminobenzotriazole-inactivated CYP2B1: Differential effects on the metabolism of 7-ethoxy-4-(trifluoromethyl)coumarin, testosterone, and benzphetamine Archives of Biochemistry and Biophysics. 423: 277-287. PMID 15001392 DOI: 10.1016/J.Abb.2004.01.007 |
0.663 |
|
| 2004 |
Ortiz-Maldonado M, Cole LJ, Dumas SM, Entsch B, Ballou DP. Increased Positive Electrostatic Potential in p-Hydroxybenzoate Hydroxylase Accelerates Hydroxylation but Slows Turnover Biochemistry. 43: 1569-1579. PMID 14769033 DOI: 10.1021/Bi030193D |
0.849 |
|
| 2003 |
Regeimbal J, Gleiter S, Trumpower BL, Yu CA, Diwakar M, Ballou DP, Bardwell JC. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proceedings of the National Academy of Sciences of the United States of America. 100: 13779-84. PMID 14612576 DOI: 10.1073/Pnas.1935988100 |
0.417 |
|
| 2003 |
Gromer S, Johansson L, Bauer H, Arscott LD, Rauch S, Ballou DP, Williams CH, Schirmer RH, Arnér ES. Active sites of thioredoxin reductases: why selenoproteins? Proceedings of the National Academy of Sciences of the United States of America. 100: 12618-23. PMID 14569031 DOI: 10.1073/Pnas.2134510100 |
0.489 |
|
| 2003 |
Ortiz-Maldonado M, Entsch B, Ballou DP. Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-Hydroxybenzoate hydroxylase Biochemistry. 42: 11234-11242. PMID 14503873 DOI: 10.1021/Bi030114Y |
0.843 |
|
| 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 |
0.659 |
|
| 2003 |
Williams CH, Ballou DP. Vincent Massey 28 November 1926 – 26 August 2002 Elected FRS 1977 Biographical Memoirs of Fellows of the Royal Society. 49: 335-350. DOI: 10.1098/Rsbm.2003.0019 |
0.418 |
|
| 2002 |
Madhavapeddi P, Ballou DP, Marsh ENG. Pre-steady-state kinetic studies on the Glu171Gln active site mutant of adenosylcobalamin-dependent glutamate mutase Biochemistry. 41: 15803-15809. PMID 12501209 DOI: 10.1021/Bi020596Y |
0.483 |
|
| 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 |
0.719 |
|
| 2002 |
Ballou DP, Zhao Y, Brandish PE, Marletta MA. Revisiting the kinetics of nitric oxide (NO) binding to soluble guanylate cyclase: The simple NO-binding model is incorrect Proceedings of the National Academy of Sciences of the United States of America. 99: 12097-12101. PMID 12209005 DOI: 10.1073/Pnas.192209799 |
0.416 |
|
| 2002 |
Palfey BA, Basu R, Frederick KK, Entsch B, Ballou DP. Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant Biochemistry. 41: 8438-8446. PMID 12081493 DOI: 10.1021/Bi012073G |
0.801 |
|
| 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 |
0.829 |
|
| 2002 |
Ballou DP, Williams CH, Coon MJ. Vincent Massey (1926–2002) Trends in Biochemical Sciences. 27: 641-642. DOI: 10.1016/S0968-0004(02)02222-3 |
0.445 |
|
| 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 |
0.59 |
|
| 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 |
0.836 |
|
| 2001 |
Trimmer EE, Ballou DP, Ludwig ML, Matthews RG. Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry. 40: 6216-26. PMID 11371182 DOI: 10.1021/Bi002790V |
0.437 |
|
| 2001 |
Trimmer EE, Ballou DP, Matthews RG. Methylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies. Biochemistry. 40: 6205-15. PMID 11371181 DOI: 10.1021/Bi002789W |
0.425 |
|
| 2001 |
Frederick KK, Ballou DP, Palfey BA. Protein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase Biochemistry. 40: 3891-3899. PMID 11300768 DOI: 10.1021/Bi001851M |
0.575 |
|
| 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 |
0.848 |
|
| 2000 |
Patil PV, Ballou DP. The use of protocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments Analytical Biochemistry. 286: 187-192. PMID 11067739 DOI: 10.1006/Abio.2000.4802 |
0.363 |
|
| 2000 |
Raner GM, Hatchell AJ, Morton PE, Ballou DP, Coon MJ. Stopped-flow spectrophotometric analysis of intermediates in the peroxo-dependent inactivation of cytochrome P450 by aldehydes. Journal of Inorganic Biochemistry. 81: 153-60. PMID 11051560 DOI: 10.1016/S0162-0134(00)00098-2 |
0.669 |
|
| 2000 |
Roymoulik I, Moon N, Dunham WR, Ballou DP, Marsh ENG. Rearrangement of L-2-hydroxyglutarate to L-threo-3-methylmalate catalyzed by adenosylcobalamin-dependent glutamate mutase Biochemistry. 39: 10340-10346. PMID 10956023 DOI: 10.1021/Bi000121B |
0.374 |
|
| 2000 |
Yanev SG, Kent UM, Roberts ES, Ballou DP, Hollenberg PF. Mechanistic studies of cytochrome P450 2B1 inactivation by xanthates Archives of Biochemistry and Biophysics. 378: 157-166. PMID 10871056 DOI: 10.1006/Abbi.2000.1807 |
0.693 |
|
| 1999 |
Coulter ED, Ballou DP. Non-haem iron-containing oxygenases involved in the microbial biodegradation of aromatic hydrocarbons. Essays in Biochemistry. 34: 31-49. PMID 10730187 DOI: 10.1042/Bse0340031 |
0.415 |
|
| 1999 |
Zhao Y, Brandish PE, Ballou DP, Marletta MA. A molecular basis for nitric oxide sensing by soluble guanylate cyclase Proceedings of the National Academy of Sciences of the United States of America. 96: 14753-14758. PMID 10611285 DOI: 10.1073/Pnas.96.26.14753 |
0.429 |
|
| 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 |
0.815 |
|
| 1999 |
Coulter ED, Moon N, Batie CJ, Dunham WR, Ballou DP. Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: direct evidence for ligation of two histidines in the copper(II)-reconstituted protein. Biochemistry. 38: 11062-72. PMID 10460161 DOI: 10.1021/Bi9904499 |
0.321 |
|
| 1999 |
Tierney DL, Gassner GT, Luchinat C, Bertini I, Ballou DP, Penner-Hahn JE. NMR characterization of substrate binding in the phthalate dioxygenase system. Biochemistry. 38: 11051-61. PMID 10460160 DOI: 10.1021/Bi990431Y |
0.359 |
|
| 1999 |
Bader M, Muse W, Ballou DP, Gassner C, Bardwell JCA. Oxidative protein folding is driven by the electron transport system Cell. 98: 217-227. PMID 10428033 DOI: 10.1016/S0092-8674(00)81016-8 |
0.357 |
|
| 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 |
0.804 |
|
| 1999 |
Moran GR, Entsch B, Palfey BA, Ballou DP. Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala. Biochemistry. 38: 6292-9. PMID 10320359 DOI: 10.1021/Bi990021+ |
0.753 |
|
| 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 |
0.749 |
|
| 1999 |
Palfey BA, Moran GR, Entsch B, Ballou DP, Massey V. Substrate recognition by "password" in p-hydroxybenzoate hydroxylase Biochemistry. 38: x-1158. |
0.697 |
|
| 1998 |
Marsh ENG, Ballou DP. Coupling of cobalt-carbon bond homolysis and hydrogen atom abstraction in adenosylcobalamin-dependent glutamate mutase Biochemistry. 37: 11864-11872. PMID 9718309 DOI: 10.1021/Bi980512E |
0.413 |
|
| 1998 |
Whittaker MM, Ballou DP, Whittaker JW. Kinetic isotope effects as probes of the mechanism of galactose oxidase Biochemistry. 37: 8426-8436. PMID 9622494 DOI: 10.1021/Bi980328T |
0.501 |
|
| 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 |
0.632 |
|
| 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 |
0.732 |
|
| 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 |
0.691 |
|
| 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 |
0.737 |
|
| 1997 |
Moran GR, Entsch B, Palfey BA, Ballou DP. Electrostatic effects on substrate activation in para-hydroxybenzoate hydroxylase: studies of the mutant lysine 297 methionine. Biochemistry. 36: 7548-56. PMID 9200706 DOI: 10.1021/Bi9706327 |
0.739 |
|
| 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 |
0.747 |
|
| 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. |
0.53 |
|
| 1996 |
Johnson DA, Gassner GT, Bandarian V, Ruzicka FJ, Ballou DP, Reed GH, Liu HW. Kinetic characterization of an organic radical in the ascarylose biosynthetic pathway. Biochemistry. 35: 15846-56. PMID 8961949 DOI: 10.1021/Bi961370W |
0.459 |
|
| 1996 |
Gottlin EB, Xu X, Epstein DM, Burke SP, Eckstein JW, Ballou DP, Dixon JE. Kinetic analysis of the catalytic domain of human cdc25B. The Journal of Biological Chemistry. 271: 27445-9. PMID 8910325 DOI: 10.1074/Jbc.271.44.27445 |
0.507 |
|
| 1996 |
Moran GR, Entsch B, Palfey BA, Ballou DP. Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys. Biochemistry. 35: 9278-85. PMID 8703933 DOI: 10.1021/Bi960360S |
0.73 |
|
| 1996 |
Sevrioukova I, Shaffer C, Ballou DP, Peterson JA. Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3. Biochemistry. 35: 7058-68. PMID 8679531 DOI: 10.1021/Bi960060A |
0.511 |
|
| 1996 |
Gurbiel RJ, Doan PE, Gassner GT, Macke TJ, Case DA, Ohnishi T, Fee JA, Ballou DP, Hoffman BM. Active site structure of Rieske-type proteins: electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center. Biochemistry. 35: 7834-45. PMID 8672484 DOI: 10.1021/Bi960380U |
0.31 |
|
| 1996 |
Gassner GT, Johnson DA, Liu HW, Ballou DP. Kinetics of the reductive half-reaction of the iron-sulfur flavoenzyme CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Biochemistry. 35: 7752-61. PMID 8672475 DOI: 10.1021/Bi960217Z |
0.404 |
|
| 1996 |
Gatti DL, Entsch B, Ballou DP, Ludwig ML. pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. Biochemistry. 35: 567-78. PMID 8555229 DOI: 10.1021/Bi951344I |
0.471 |
|
| 1996 |
Tsang HT, Batie CJ, Ballou DP, Penner-Hahn JE. Structural characterization of the mononuclear iron site in Pseudomonas cepacia phthalate DB10 dioxygenase using X-ray absorption spectroscopy Journal of Biological Inorganic Chemistry. 1: 24-33. DOI: 10.1007/S007750050019 |
0.33 |
|
| 1995 |
Gassner GT, Ludwig ML, Gatti DL, Correll CC, Ballou DP. Structure and mechanism of the iron-sulfur flavoprotein phthalate dioxygenase reductase. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1411-8. PMID 7589982 DOI: 10.1096/Fasebj.9.14.7589982 |
0.386 |
|
| 1995 |
Gassner GT, Ballou DP. Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain. Biochemistry. 34: 13460-71. PMID 7577934 DOI: 10.1021/Bi00041A025 |
0.437 |
|
| 1995 |
Roberts ES, Ballou DP, Hopkins NE, Alworth WL, Hollenberg PF. Mechanistic studies of 9-ethynylphenanthrene-inactivated cytochrome P450 2B1. Archives of Biochemistry and Biophysics. 323: 303-12. PMID 7487092 DOI: 10.1006/Abbi.1995.9960 |
0.648 |
|
| 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 |
0.693 |
|
| 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 |
0.653 |
|
| 1994 |
Gassner G, Wang L, Batie C, Ballou DP. Reaction of phthalate dioxygenase reductase with NADH and NAD: kinetic and spectral characterization of intermediates. Biochemistry. 33: 12184-93. PMID 7522555 DOI: 10.1021/Bi00206A022 |
0.455 |
|
| 1993 |
Xu F, DeFilippi LJ, Ballou DP, Hultquist DE. Hydrogen peroxide-dependent formation and bleaching of the higher oxidation states of bovine erythrocyte green hemeprotein. Archives of Biochemistry and Biophysics. 301: 184-9. PMID 8442660 DOI: 10.1006/Abbi.1993.1131 |
0.45 |
|
| 1993 |
Gassner GT, Ballou DP, Landrum GA, Whittaker JW. Magnetic circular dichroism studies on the mononuclear ferrous active site of phthalate dioxygenase from Pseudomonas cepacia show a change of ligation state on substrate binding Biochemistry. 32: 4820-4825. PMID 7683910 DOI: 10.1021/Bi00069A017 |
0.379 |
|
| 1992 |
Correll CC, Batie CJ, Ballou DP, Ludwig ML. Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science (New York, N.Y.). 258: 1604-10. PMID 1280857 DOI: 10.1126/Science.1280857 |
0.327 |
|
| 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 |
0.639 |
|
| 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 |
0.659 |
|
| 1991 |
Cole JL, Ballou DP, Solomon EI. Spectroscopic characterization of the peroxide intermediate in the reduction of dioxygen catalyzed by the multicopper oxidases Journal of the American Chemical Society. 113: 8544-8546. DOI: 10.1021/Ja00022A064 |
0.481 |
|
| 1991 |
Cole JL, Ballou DP, Solomon EI. Spectroscopic characterization of the Peroxide intermediate in the reduction of dioxygen catalyzed by the multicopper oxidases Journal of the American Chemical Society. 113: 8544-8546. |
0.38 |
|
| 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 |
0.545 |
|
| 1990 |
Banerjee RV, Frasca V, Ballou DP, Matthews RG. Participation of cob(I) alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry. 29: 11101-9. PMID 2271698 DOI: 10.1021/Bi00502A013 |
0.486 |
|
| 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 |
0.682 |
|
| 1989 |
Powlowski J, Massey V, Ballou DP. Reactions of anthranilate hydroxylase with salicylate, a nonhydroxylated substrate analogue. Steady state and rapid reaction kinetics Journal of Biological Chemistry. 264: 5606-5612. PMID 2925623 |
0.458 |
|
| 1989 |
Zylstra GJ, Olsen RH, Ballou DP. Cloning, expression, and regulation of the Pseudomonas cepacia protocatechuate 3,4-dioxygenase genes. Journal of Bacteriology. 171: 5907-14. PMID 2808302 DOI: 10.1128/Jb.171.11.5907-5914.1989 |
0.385 |
|
| 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 |
0.667 |
|
| 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 |
0.638 |
|
| 1989 |
Entsch B, Ballou DP. Purification, properties, and oxygen reactivity of p-hydroxybenzoate hydroxylase from Pseudomonas aeruginosa Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 999: 313-322. PMID 2513888 DOI: 10.1016/0167-4838(89)90014-9 |
0.564 |
|
| 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 |
0.517 |
|
| 1988 |
Green JM, Ballou DP, Matthews RG. Examination of the role of methylenetetrahydrofolate reductase in incorporation of methyltetrahydrofolate into cellular metabolism Faseb Journal. 2: 42-47. PMID 3335280 DOI: 10.1096/Fasebj.2.1.3335280 |
0.347 |
|
| 1987 |
Powlowski JB, Dagley S, Massey V, Ballou DP. Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum Journal of Biological Chemistry. 262: 69-74. PMID 3793735 |
0.405 |
|
| 1986 |
Jones KC, Ballou DP. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates Journal of Biological Chemistry. 261: 2553-2559. PMID 3949735 |
0.377 |
|
| 1986 |
Roberts DD, Lewis SD, Ballou DP, Olson ST, Shafer JA. Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate Biochemistry. 25: 5595-5601. PMID 3778876 DOI: 10.1021/Bi00367A038 |
0.414 |
|
| 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 |
0.624 |
|
| 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 |
0.606 |
|
| 1985 |
Correll CC, Batie CJ, Ballou DP, Ludwig ML. Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia. The Journal of Biological Chemistry. 260: 14633-5. PMID 2997216 |
0.314 |
|
| 1983 |
Walsh TA, Ballou DP, Mayer R, Que L. Rapid reaction studies on the oxygenation reactions of catechol dioxygenase. Journal of Biological Chemistry. 258: 14422-14427. PMID 6643492 |
0.452 |
|
| 1983 |
Walsh TA, Ballou DP. Halogenated protocatechuates as substrates for protocatechuate dioxygenase from Pseudomonas cepacia. Journal of Biological Chemistry. 258: 14413-14421. PMID 6643491 |
0.391 |
|
| 1983 |
Vanoni MA, Ballou DP, Matthews RG. Methylenetetrahydrofolate reductase. Steady state and rapid reaction studies on the NADPH-methylenetetrahydrofolate, NADPH-menadione, and methyltetrahydrofolate-menadione oxidoreductase activities of the enzyme Journal of Biological Chemistry. 258: 11510-11514. PMID 6352699 |
0.418 |
|
| 1982 |
Ryerson CC, Ballou DP, Walsh C. Mechanistic studies on cyclohexanone oxygenase Biochemistry. 21: 2644-2655. PMID 7093214 DOI: 10.1021/Bi00540A011 |
0.502 |
|
| 1982 |
Ryerson CC, Ballou DP, Walsh C. Kinetic isotope effects in the oxidation of isotopically labeled NAD(P)H by bacterial flavoprotein monooxygenases Biochemistry. 21: 1144-1151. PMID 7074071 DOI: 10.1021/Bi00535A006 |
0.41 |
|
| 1981 |
Bull C, Ballou DP, Otsuka S. The reaction of oxygen with protocatechuate 3,4-dioxygenase from Pseudomonas putida. Characterization of a new oxygenated intermediate Journal of Biological Chemistry. 256: 12681-12686. PMID 7309730 |
0.378 |
|
| 1981 |
Beaty NB, Ballou DP. The oxidative half-reaction of liver microsomal FAD-containing monooxygenase Journal of Biological Chemistry. 256: 4619-4625. PMID 7217103 |
0.415 |
|
| 1981 |
Beaty NB, Ballou DP. The reductive half-reaction of liver microsomal FAD-containing monooxygenase Journal of Biological Chemistry. 256: 4611-4618. PMID 7217102 |
0.415 |
|
| 1981 |
Vermilion JL, Ballou DP, Massey V, Coon MJ. Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase Journal of Biological Chemistry. 256: 266-277. PMID 6778861 |
0.668 |
|
| 1980 |
Ruckpaul K, Rein H, Ballou DP, Coon MJ. Analysis of interactions among purified components of the liver microsomal cytochrome P-450-containing monooxygenase system by second derivative spectroscopy. Biochimica Et Biophysica Acta. 626: 41-56. PMID 7459382 DOI: 10.1016/0005-2795(80)90195-6 |
0.585 |
|
| 1980 |
Beaty NB, Ballou DP. Transient kinetic study of liver microsomal FAD-containing monooxygenase Journal of Biological Chemistry. 255: 3817-3819. PMID 7372647 |
0.376 |
|
| 1980 |
Husain M, Entsch B, Ballou DP, Massey V, Chapman PJ. Fluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase Journal of Biological Chemistry. 255: 4189-4197. PMID 6768750 |
0.417 |
|
| 1980 |
Entsch B, Husain M, Ballou DP, Massey V, Walsh C. Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD Journal of Biological Chemistry. 255: 1420-1429. PMID 6766449 |
0.495 |
|
| 1980 |
Vermilion JL, Massey V, Ballou DP, Coon MJ. Cytochrome P-450 Reduction By Fmn-Depleted Rat Liver Nadph-Cytochrome P-450 Reductase Reconstituted With Artificial Flavins Microsomes, Drug Oxidations and Chemical Carcinogenesis. 379-382. DOI: 10.1016/B978-0-12-187701-9.50075-9 |
0.672 |
|
| 1980 |
Beaty N, Ballou D. A Kinetic Investigation Of Liver Microsomal Mixed Function Amine Oxidase Microsomes, Drug Oxidations and Chemical Carcinogenesis. 299-302. DOI: 10.1016/B978-0-12-187701-9.50055-3 |
0.472 |
|
| 1980 |
Ruckpaul K, Rein H, Ballou DP, Coon MJ. Second Derivative Spectroscopic Studies Of The Essential Components Of The Liver Microsomal Monooxygenation System Microsomes, Drug Oxidations and Chemical Carcinogenesis. 37-45. DOI: 10.1016/B978-0-12-187701-9.50009-7 |
0.582 |
|
| 1979 |
Coon MJ, Blake RC, Oprian DD, Ballou DP. Mechanistic studies with purified components of the liver microsomal hydroxylation system: spectral intermediates in reaction of cytochrome P-450 with peroxy compounds. Acta Biologica Et Medica Germanica. 38: 449-58. PMID 42250 |
0.786 |
|
| 1977 |
Matthews RG, Ballou DP, Thorpe C, Williams CH. Ion pair formation in pig heart lipoamide dehydrogenase: rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide. The Journal of Biological Chemistry. 252: 3199-207. PMID 16887 |
0.316 |
|
| 1976 |
Coon MJ, Ballou DP, Guengerich FP, Nordblom GD, White RE. Highly purified cytochrome P-450 from liver microsomal membranes: recent studies on the mechanism of catalysis Advances in Experimental Medicine and Biology. 74: 270-280. PMID 961532 DOI: 10.1007/978-1-4684-3270-1_20 |
0.629 |
|
| 1976 |
Peter Guengerich F, Ballou DP, Coon MJ. Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450 Biochemical and Biophysical Research Communications. 70: 951-956. PMID 938535 DOI: 10.1016/0006-291X(76)90684-7 |
0.668 |
|
| 1976 |
Entsch B, Ballou DP, Husain M, Massey V. Catalytic mechanism of p hydroxybenzoate hydroxylase with p mercaptobenzoate as substrate Journal of Biological Chemistry. 251: 7367-7379. PMID 826528 |
0.499 |
|
| 1976 |
Entsch B, Ballou DP, Massey V. Flavin oxygen derivatives involved in hydroxylation by p hydroxybenzoate hydroxylase Journal of Biological Chemistry. 251: 2550-2563. PMID 816794 |
0.484 |
|
| 1975 |
Guengerich FP, Ballou DP, Coon MJ. Purified liver microsomal cytochrome P 450. Electron accepting properties and oxidation reduction potential Journal of Biological Chemistry. 250: 7405-7414. PMID 1165247 |
0.654 |
|
| 1975 |
Coon MJ, van der Hoeven A, Haugen DA, Guengerich FP, Vermilion JL, Ballou DP. Biochemical characterization of highly purified cytochrome P-450 and other components of the mixed function oxidase system of liver microsomal membranes. Advances in Experimental Medicine and Biology. 58: 25-46. PMID 168750 DOI: 10.1007/978-1-4615-9026-2_2 |
0.688 |
|
| 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 |
0.651 |
|
| 1974 |
Ballou DP, Veeger C, van der Hoeven TA, Coon MJ. Properties of partially purified liver microsomal cytochrome P-450: Acceptance of two electrons during anaerobic titration Febs Letters. 38: 337-340. PMID 4369075 DOI: 10.1016/0014-5793(74)80086-4 |
0.565 |
|
| 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 |
0.574 |
|
| 1974 |
Ballou DP, Palmer GA. Practical rapid quenching instrument for the study of reaction mechanisms by electron paramagnetic resonance spectroscopy Analytical Chemistry. 46: 1248-1253. DOI: 10.1021/Ac60345A034 |
0.519 |
|
| 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 |
0.677 |
|
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