| Year |
Citation |
Score |
| 2007 |
Bhattacharyya S, Stankovich MT, Truhlar DG, Gao J. Combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor in water, medium-chain acyl-CoA dehydrogenase, and cholesterol oxidase. The Journal of Physical Chemistry. A. 111: 5729-42. PMID 17567113 DOI: 10.1021/Jp071526+ |
0.538 |
|
| 2005 |
Bhattacharyya S, Ma S, Stankovich MT, Truhlar DG, Gao J. Potential of mean force calculation for the proton and hydride transfer reactions catalyzed by medium-chain acyl-CoA dehydrogenase: effect of mutations on enzyme catalysis. Biochemistry. 44: 16549-62. PMID 16342946 DOI: 10.1021/Bi051630M |
0.519 |
|
| 2005 |
Saenger AK, Nguyen TV, Vockley J, Stankovich MT. Thermodynamic regulation of human short-chain acyl-CoA dehydrogenase by substrate and product binding. Biochemistry. 44: 16043-53. PMID 16331964 DOI: 10.1021/Bi051048Y |
0.752 |
|
| 2005 |
Saenger AK, Nguyen TV, Vockley J, Stankovich MT. Biochemical and electrochemical characterization of two variant human short-chain acyl-CoA dehydrogenases. Biochemistry. 44: 16035-42. PMID 16331963 DOI: 10.1021/Bi051049Q |
0.741 |
|
| 2004 |
Zlateva T, Quaroni L, Que L, Stankovich MT. Redox studies of subunit interactivity in aerobic ribonucleotide reductase from Escherichia coli. The Journal of Biological Chemistry. 279: 18742-7. PMID 14966112 DOI: 10.1074/Jbc.M311355200 |
0.345 |
|
| 2003 |
Wu J, Bell AF, Luo L, Stephens AW, Stankovich MT, Tonge PJ. Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy. Biochemistry. 42: 11846-56. PMID 14529297 DOI: 10.1021/Bi0344578 |
0.745 |
|
| 2003 |
Lamm TR, Kohls TD, Saenger AK, Stankovich MT. Comparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes. Archives of Biochemistry and Biophysics. 409: 251-61. PMID 12504892 DOI: 10.1016/S0003-9861(02)00632-X |
0.758 |
|
| 2002 |
Lamm TR, Kohls TD, Stankovich MT. Activation of substrate/product couples by medium-chain acyl-CoA dehydrogenase. Archives of Biochemistry and Biophysics. 404: 136-46. PMID 12127078 DOI: 10.1016/S0003-9861(02)00229-1 |
0.768 |
|
| 2002 |
Faro M, Gómez-Moreno C, Stankovich M, Medina M. Role of critical charged residues in reduction potential modulation of ferredoxin-NADP+ reductase. Febs Journal. 269: 2656-2661. PMID 12047373 DOI: 10.1046/J.1432-1033.2002.02925.X |
0.473 |
|
| 2001 |
Pellett JD, Becker DF, Saenger AK, Fuchs JA, Stankovich MT. Role of aromatic stacking interactions in the modulation of the two-electron reduction potentials of flavin and substrate/product in Megasphaera elsdenii short-chain acyl-coenzyme A dehydrogenase. Biochemistry. 40: 7720-8. PMID 11412126 DOI: 10.1021/Bi010206S |
0.779 |
|
| 2001 |
Martínez-Júlvez M, Nogués I, Faro M, Hurley JK, Brodie TB, Mayoral T, Sanz-Aparicio J, Hermoso JA, Stankovich MT, Medina M, Tollin G, Gómez-Moreno C. Role of a Cluster of Hydrophobic Residues Near the FAD Cofactor in Anabaena PCC 7119 Ferredoxin-NADP+ Reductase for Optimal Complex Formation and Electron Transfer to Ferredoxin Journal of Biological Chemistry. 276: 27498-27510. PMID 11342548 DOI: 10.1074/Jbc.M102112200 |
0.478 |
|
| 2000 |
Pellett JD, Sabaj KM, Stephens AW, Bell AF, Wu J, Tonge PJ, Stankovich MT. Medium-chain acyl-coenzyme A dehydrogenase bound to a product analogue, hexadienoyl-coenzyme A: effects on reduction potential, pK(a), and polarization. Biochemistry. 39: 13982-92. PMID 11076541 DOI: 10.1021/Bi0006464 |
0.801 |
|
| 1999 |
Stankovich MT, Sabaj KM, Tonge PJ. Structure/function of medium chain Acyl-CoA dehydrogenase: The importance of substrate polarization Archives of Biochemistry and Biophysics. 370: 16-21. PMID 10496972 DOI: 10.1006/Abbi.1999.1385 |
0.411 |
|
| 1999 |
Miller MA, Gobena FT, Kauffmann K, Münck E, Que L, Stankovich MT. Differing roles for the diiron clusters of ribonucleotide reductase from aerobically grown Escherichia coli in the generation of the Y122 radical [5] Journal of the American Chemical Society. 121: 1096-1097. DOI: 10.1021/Ja9826845 |
0.3 |
|
| 1998 |
Mancini-Samuelson GJ, Kieweg V, Sabaj KM, Ghisla S, Stankovich MT. Redox properties of human medium-chain Acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues Biochemistry. 37: 14605-14612. PMID 9772189 DOI: 10.1021/Bi981414W |
0.5 |
|
| 1998 |
Weber-Main AM, Hurley JK, Cheng H, Xia B, Chae YK, Markley JL, Martinez-Júlvez M, Gomez-Moreno C, Stankovich MT, Tollin G. An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop. Archives of Biochemistry and Biophysics. 355: 181-8. PMID 9675025 DOI: 10.1006/Abbi.1998.0743 |
0.437 |
|
| 1998 |
DuPlessis ER, Pellett J, Stankovich MT, Thorpe C. Oxidase activity of the acyl-CoA dehydrogenases Biochemistry. 37: 10469-10477. PMID 9671517 DOI: 10.1021/Bi980767S |
0.807 |
|
| 1998 |
Presta A, Weber-Main AM, Stankovich MT, Stuehr DJ. Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthases Journal of the American Chemical Society. 120: 9460-9465. DOI: 10.1021/Ja9740374 |
0.475 |
|
| 1997 |
Hurley JK, Weber-Main AM, Hodges AE, Stankovich MT, Benning MM, Holden HM, Cheng H, Xia B, Markley JL, Genzor C, Gomez-Moreno C, Hafezi R, Tollin G. Iron-sulfur cluster cysteine-to-serine mutants of Anabaena -2Fe-2S- ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP+ reductase. Biochemistry. 36: 15109-17. PMID 9398238 DOI: 10.1021/Bi972001I |
0.401 |
|
| 1997 |
Hurley JK, Weber-Main AM, Stankovich MT, Benning MM, Thoden JB, Vanhooke JL, Holden HM, Chae YK, Xia B, Cheng H, Markley JL, Martinez-Júlvez M, Gómez-Moreno C, Schmeits JL, Tollin G. Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants. Biochemistry. 36: 11100-17. PMID 9287153 DOI: 10.1021/Bi9709001 |
0.458 |
|
| 1997 |
Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD. Roles of the methane monooxygenase reductase component in the regulation of catalysis. Biochemistry. 36: 5223-33. PMID 9136884 DOI: 10.1021/Bi962743W |
0.514 |
|
| 1996 |
Burns KD, Pieper PA, Liu HW, Stankovich MT. Studies of the redox properties of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) and CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase (E3): Two important enzymes involved in the biosynthesis of ascarylose Biochemistry. 35: 7879-7889. PMID 8672489 DOI: 10.1021/Bi960284T |
0.391 |
|
| 1996 |
Eng LH, Schlegel V, Wang DL, Neujahr HY, Stankovich MT, Cotton T. Resonance Raman scattering and surface-enhanced resonance Raman scattering studies of oxido-reduction of cytochrome c3 Langmuir. 12: 3055-3059. DOI: 10.1021/La950599U |
0.329 |
|
| 1996 |
Dakoji S, Shin I, Becker DF, Stankovich MT, Liu HW. Studies of acyl-CoA dehydrogenase catalyzed allylic isomerization: A one-base or two-base mechanism? Journal of the American Chemical Society. 118: 10971-10979. DOI: 10.1021/Ja962532E |
0.674 |
|
| 1995 |
Djordjevic S, Pace CP, Stankovich MT, Kim JJP. Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii Biochemistry. 34: 2163-2171. PMID 7857927 DOI: 10.1021/Bi00007A009 |
0.509 |
|
| 1995 |
Johnson BD, Mancini-Samuelson GJ, Stankovich MT. Effect of transition-state analogues on the redox properties of medium-chain acyl-CoA dehydrogenase Biochemistry. 34: 7047-7055. PMID 7766614 DOI: 10.1021/Bi00021A016 |
0.525 |
|
| 1995 |
Silva KE, Elgren TE, Que L, Stankovich MT. Electron transfer properties of the R2 protein of ribonucleotide reductase from Escherichia coli Biochemistry. 34: 14093-14103. PMID 7578006 DOI: 10.1021/Bi00043A014 |
0.393 |
|
| 1994 |
Paulsen KE, Liu Y, Fox BG, Lipscomb JD, Münck E, Stankovich MT. Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry. 33: 713-22. PMID 8292599 DOI: 10.1021/Bi00169A013 |
0.41 |
|
| 1994 |
Pace CP, Stankovich MT. Oxidation-reduction properties of short-chain acyl-CoA dehydrogenase: Effects of substrate analogs Archives of Biochemistry and Biophysics. 313: 261-266. PMID 8080271 DOI: 10.1006/Abbi.1994.1386 |
0.529 |
|
| 1994 |
Becker DF, Fuchs JA, Stankovich MT. Product binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant Biochemistry. 33: 7082-7087. PMID 8003473 DOI: 10.1021/Bi00189A010 |
0.751 |
|
| 1994 |
Shin I, Li D, Becker DF, Stankovich MT, Liu H. Cyclobutaneacetyl-CoA: A Janus-faced substrate for acyl-CoA dehydrogenases Journal of the American Chemical Society. 116: 8843-8844. DOI: 10.1021/Ja00098A068 |
0.648 |
|
| 1993 |
Stankovich MT. Influence of two substrate analogues on thermodynamic properties of medium-chain Acyl-CoA dehydrogenase Biochemistry. 32: 10779-10785. PMID 8399226 DOI: 10.1021/Bi00091A032 |
0.507 |
|
| 1993 |
Stankovich MT. Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from megasphaera elsdenii Biochemistry. 32: 10736-10742. PMID 8399220 DOI: 10.1021/Bi00091A026 |
0.376 |
|
| 1993 |
Silva K, Stankovich M, Que L. Electron transfer properties of the small subunit R2 of ribonucleotide reductase from E. coli. Journal of Inorganic Biochemistry. 51: 306. DOI: 10.1016/0162-0134(93)85338-9 |
0.346 |
|
| 1993 |
Liu Y, Paulsen KE, Stankovich MT, Lipscomb JD. Regulation of methane monooxygenase catalysis through thermodynamic coupling of redox equilibria and component complexes Journal of Inorganic Biochemistry. 51: 37. DOI: 10.1016/0162-0134(93)85075-J |
0.323 |
|
| 1993 |
Weber-Main A, Cheng H, Xia B, Stankovich M, Markley J. Comparison of the thermodynamic electrochemical properties of wild-type and mutant [2Fe2S] ferredoxins from Anabaena 7120 Journal of Inorganic Biochemistry. 51: 31. DOI: 10.1016/0162-0134(93)85069-K |
0.302 |
|
| 1992 |
Johnson BD, Stankovich MT. Thermodynamic studies of medium-chain acyl-CoA dehydrogenase complexed to thioether-CoA ligands Progress in Clinical and Biological Research. 375: 63-68. PMID 1438402 |
0.313 |
|
| 1992 |
Paulsen KE, Orville AM, Frerman FE, Lipscomb JD, Stankovich MT. Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry. 31: 11755-61. PMID 1332770 DOI: 10.1021/Bi00162A012 |
0.406 |
|
| 1991 |
Pace CP, Stankovich MT. Oxidation-reduction properties of trimethylamine dehydrogenase: Effect of inhibitor binding Archives of Biochemistry and Biophysics. 287: 97-104. PMID 1897998 DOI: 10.1016/0003-9861(91)90393-W |
0.45 |
|
| 1991 |
Wang DL, Holz RC, David SS, Que L, Stankovich MT. Electrochemical properties of the diiron core of uteroferrin and its anion complexes. Biochemistry. 30: 8187-94. PMID 1868093 DOI: 10.1021/Bi00247A014 |
0.425 |
|
| 1991 |
Paulsen K, Stankovich M, Orville A, Lipscomb J, Frerman F. The redox and spectroscopic properties of ETF-ubiquinone oxidoreductase. Journal of Inorganic Biochemistry. 43: 256. DOI: 10.1016/0162-0134(91)84246-6 |
0.349 |
|
| 1991 |
Wang DL, Stankovich MT, Eng LH, Neujahr HY. Redox properties of cytochrome c3 from Desulfovibrio desulfuricans NCIMB 8372. Effects of electrode materials and sodium chloride Journal of Electroanalytical Chemistry. 318: 291-307. DOI: 10.1016/0022-0728(91)85311-C |
0.395 |
|
| 1990 |
Lenn ND, Stankovich MT, Liu HW. Regulation of the redox potential of general acyl-CoA dehydrogenase by substrate binding Biochemistry. 29: 3709-3715. PMID 2340267 DOI: 10.1021/Bi00467A017 |
0.568 |
|
| 1990 |
Byron CM, Stankovich MT, Husain M. Spectral and electrochemical properties of glutaryl-CoA dehydrogenase from Paracoccus denitrificans Biochemistry. 29: 3691-3700. PMID 2340266 DOI: 10.1021/Bi00467A015 |
0.808 |
|
| 1990 |
Lenn ND, Liu HW, Stankovich MT. Regulation of electron transfer to general acyl-CoA dehydrogenase by substrate binding Progress in Clinical and Biological Research. 321: 123-128. PMID 2326289 |
0.397 |
|
| 1990 |
Paulsen KE, Stankovich MT, Stockman BJ, Markley JL. Redox and spectral properties of flavodoxin from Anabaena 7120. Archives of Biochemistry and Biophysics. 280: 68-73. PMID 2112901 DOI: 10.1016/0003-9861(90)90519-5 |
0.374 |
|
| 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 |
0.576 |
|
| 1989 |
Byron CM, Stankovich MT, Husain M, Davidson VL. Unusual redox properties of electron-transfer flavoprotein from methylophilus methylotrophus Biochemistry. 28: 8582-8587. PMID 2605209 DOI: 10.1021/Bi00447A047 |
0.763 |
|
| 1989 |
Millis CD, Cai D, Stankovich MT, Tien M. Oxidation-reduction potentials and ionization states of extracellular peroxidases from the lignin-degrading fungus phanerochaete chrysosporium Biochemistry. 28: 8484-8489. PMID 2605198 DOI: 10.1021/Bi00447A032 |
0.339 |
|
| 1989 |
Lenn ND, Shih Y, Stankovich MT, Liu HW. Studies of the inactivation of General Acyl-CoA Dehydrogenase by racemic (methylenecyclopropyl)acetyl-CoA: New evidence suggesting a radical mechanism of this enzyme-catalyzed reaction Journal of the American Chemical Society. 111: 3065-3067. DOI: 10.1021/Ja00190A051 |
0.459 |
|
| 1988 |
Einarsdottir GH, Stankovich MT, Tu SC. Studies of electron-transfer properties of salicylate hydroxylase from Pseudomonas cepacia and effects of salicylate and benzoate binding. Biochemistry. 27: 3277-85. PMID 3390431 DOI: 10.1021/Bi00409A023 |
0.558 |
|
| 1987 |
Pace CP, Stankovich MT. Redox properties of electron-transferring flavoprotein from Megasphaera elsdenii Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 267-276. PMID 3814604 DOI: 10.1016/0167-4838(87)90067-7 |
0.417 |
|
| 1987 |
Soltysik S, Byron CM, Einarsdottir GH, Stankovich MT. The effects of reversible freezing inactivation and inhibitor binding on redox properties of l-amino-acid oxidase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 201-208. PMID 3801494 DOI: 10.1016/0167-4838(87)90009-4 |
0.769 |
|
| 1987 |
Stankovich MT, Soltysik S. Regulation of the butyryl-CoA dehydrogenase by substrate and product binding Biochemistry. 26: 2627-2632. PMID 3607039 DOI: 10.1021/Bi00383A033 |
0.572 |
|
| 1986 |
Fink CW, Stankovich MT, Soltysik S. Oxidation-reduction potentials of butyryl-CoA dehydrogenase Biochemistry. 25: 6637-6643. PMID 3790549 DOI: 10.1021/Bi00369A046 |
0.581 |
|
| 1986 |
Pace C, Stankovich M. Oxidation-reduction properties of glycolate oxidase. Biochemistry. 25: 2516-22. PMID 3521736 DOI: 10.1021/Bi00357A035 |
0.379 |
|
| 1985 |
Van den Berghe-Snorek S, Stankovich MT. Thermodynamic control of D-amino acid oxidase by benzoate binding Journal of Biological Chemistry. 260: 3373-3379. PMID 2857720 |
0.43 |
|
| 1984 |
Husain M, Stankovich MT, Fox BG. Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver. The Biochemical Journal. 219: 1043-7. PMID 6743239 DOI: 10.1042/Bj2191043 |
0.401 |
|
| 1984 |
Stankovich MT, Fox BG. Redox potential-pH properties of the flavoprotein L-amino-acid oxidase. Biochimica Et Biophysica Acta. 786: 49-56. PMID 6712956 DOI: 10.1016/0167-4838(84)90152-3 |
0.412 |
|
| 1984 |
Van Den Berghe-Snorek S, Stankovich MT. Thermodynamic control of electron transfer of flavoproteins by substrate binding Journal of the American Chemical Society. 106: 3685-3687. DOI: 10.1021/Ja00324A055 |
0.437 |
|
| 1983 |
Stankovich M, Fox B. Redox potentials of the flavoprotein lactate oxidase. Biochemistry. 22: 4466-72. PMID 6626511 DOI: 10.1021/Bi00288A018 |
0.48 |
|
| 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 |
0.436 |
|
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