| Year |
Citation |
Score |
| 2020 |
Mamounis KJ, Yukl ET, Davidson VL. Roles of active site residues in catalysis, substrate binding, cooperativity and the reaction mechanism of the quinoprotein glycine oxidase. The Journal of Biological Chemistry. PMID 32234764 DOI: 10.1074/Jbc.Ra120.013198 |
0.48 |
|
| 2020 |
Ma Z, Abendroth J, Buchko GW, Rohde KH, Davidson VL. Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis. The Biochemical Journal. PMID 31913442 DOI: 10.1042/Bcj20190827 |
0.372 |
|
| 2019 |
Mamounis KJ, Avalos D, Yukl ET, Davidson VL. Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase. The Journal of Biological Chemistry. PMID 31615898 DOI: 10.1074/Jbc.Ra119.011255 |
0.49 |
|
| 2019 |
Mamounis KJ, Ma Z, Sanchez-Amat A, Davidson VL. Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea. Archives of Biochemistry and Biophysics. 108110. PMID 31541619 DOI: 10.1016/J.Abb.2019.108110 |
0.432 |
|
| 2019 |
Ma Z, Davidson VL. Redox properties of a cysteine tryptophylquinone-dependent glycine oxidase are distinct from those of tryptophylquinone-dependent dehydrogenases. Biochemistry. PMID 30945853 DOI: 10.1021/Acs.Biochem.9B00104 |
0.403 |
|
| 2019 |
Avalos D, Sabuncu S, Mamounis KJ, Davidson VL, Moënne-Loccoz P, Yukl ET. Structural and spectroscopic characterization of a product Schiff-base intermediate in the reaction of the quinoprotein glycine oxidase, GoxA. Biochemistry. PMID 30605596 DOI: 10.1021/Acs.Biochem.8B01145 |
0.443 |
|
| 2018 |
Yukl ET, Davidson VL. Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes. Archives of Biochemistry and Biophysics. 654: 40-46. PMID 30026025 DOI: 10.1016/J.Abb.2018.07.012 |
0.404 |
|
| 2018 |
Davidson VL. Protein-derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions. Biochemistry. PMID 29498828 DOI: 10.1021/Acs.Biochem.8B00123 |
0.462 |
|
| 2018 |
Andreo-Vidal A, Mamounis K, Sehanobish E, Avalos D, Campillo-Brocal JC, Sanchez-Amat A, Yukl ET, Davidson VL. Structure and enzymatic properties of an unusual cysteine tryptophylquinone-dependent glycine oxidase from Pseudoalteromonas luteoviolacea. Biochemistry. PMID 29381339 DOI: 10.1021/Acs.Biochem.8B00009 |
0.435 |
|
| 2017 |
Ma Z, Strickland KT, Cherne MD, Sehanobish E, Rohde KH, Self WT, Davidson VL. The Rv2633c protein of Mycobacterium tuberculosis is a non-heme di-iron catalase with a possible role in defenses against oxidative stress. The Journal of Biological Chemistry. PMID 29242190 DOI: 10.1074/Jbc.Ra117.000421 |
0.356 |
|
| 2017 |
Ma Z, Davidson VL. Ascorbate Protects the Di-Heme Enzyme, MauG, Against Self-Inflicted Oxidative Damage by an Unusual Antioxidant Mechanism. The Biochemical Journal. PMID 28634178 DOI: 10.1042/Bcj20170349 |
0.49 |
|
| 2017 |
Feng M, Ma Z, Crudup BF, Davidson VL. Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away. Febs Letters. PMID 28485817 DOI: 10.1002/1873-3468.12666 |
0.43 |
|
| 2017 |
Williamson HR, Sehanobish E, Shiller AM, Sanchez-Amat A, Davidson VL. Roles of copper and a conserved aspartic acid in the autocatalytic hydroxylation of a specific tryptophan residue during cysteine tryptophylquinone biogenesis. Biochemistry. PMID 28140566 DOI: 10.1021/Acs.Biochem.6B01137 |
0.739 |
|
| 2017 |
Sehanobish E, Dow BA, Davidson VL. Analytical Methods for Assessing the Effects of Site-Directed Mutagenesis on Protein-Cofactor and Protein-Protein Functional Relationships. Methods in Molecular Biology (Clifton, N.J.). 1498: 421-438. PMID 27709593 DOI: 10.1007/978-1-4939-6472-7_29 |
0.396 |
|
| 2017 |
Dow BA, Sehanobish E, Davidson VL. In Silico Approaches to Identify Mutagenesis Targets to Probe and Alter Protein-Cofactor and Protein-Protein Functional Relationships. Methods in Molecular Biology (Clifton, N.J.). 1498: 181-190. PMID 27709576 DOI: 10.1007/978-1-4939-6472-7_12 |
0.351 |
|
| 2016 |
Sehanobish E, Williamson HR, Davidson VL. Roles of conserved residues of GoxA in controlling glycine oxidase activity, cooperativity, subunit composition and cysteine tryptophylquinone biosynthesis. The Journal of Biological Chemistry. PMID 27637328 DOI: 10.1074/Jbc.M116.741835 |
0.742 |
|
| 2016 |
Ma Z, Williamson HR, Davidson VL. A suicide mutation affecting proton transfers to high-valent hemes causes inactivation of MauG during catalysis. Biochemistry. PMID 27622473 DOI: 10.1021/Acs.Biochem.6B00816 |
0.747 |
|
| 2016 |
Ma Z, Williamson HR, Davidson VL. Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent hemes. The Biochemical Journal. PMID 27076451 DOI: 10.1042/Bcj20160047 |
0.755 |
|
| 2016 |
Sehanobish E, Camprillo-Brocal JC, Williamson HR, Sanchez-Amat A, Davidson VL. Interaction of GoxA with its modifying enzyme and its subunit assembly are dependent on the extent of cysteine tryptophylquinone biosynthesis. Biochemistry. PMID 27064961 DOI: 10.1021/Acs.Biochem.6B00274 |
0.723 |
|
| 2016 |
Dow BA, Davidson VL. Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer. The Biochemical Journal. 473: 67-72. PMID 26494530 DOI: 10.1042/Bj20150998 |
0.437 |
|
| 2015 |
Ma Z, Williamson HR, Davidson VL. Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG. Proceedings of the National Academy of Sciences of the United States of America. 112: 10896-901. PMID 26283395 DOI: 10.1073/Pnas.1510986112 |
0.724 |
|
| 2015 |
Dow BA, Davidson VL. Characterization of the free energy dependence of an interprotein electron transfer reaction by variation of pH and site-directed mutagenesis. Biochimica Et Biophysica Acta. 1847: 1181-6. PMID 26087387 DOI: 10.1016/J.Bbabio.2015.06.012 |
0.421 |
|
| 2015 |
Sehanobish E, Chacón-Verdú MD, Sanchez-Amat A, Davidson VL. Roles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidase. Archives of Biochemistry and Biophysics. 579: 26-32. PMID 26048732 DOI: 10.1016/J.Abb.2015.05.013 |
0.406 |
|
| 2015 |
Shin S, Feng M, Li C, Williamson HR, Choi M, Wilmot CM, Davidson VL. A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state. Biochimica Et Biophysica Acta. 1847: 709-16. PMID 25896561 DOI: 10.1016/J.Bbabio.2015.04.008 |
0.787 |
|
| 2015 |
Dow BA, Tatulian SA, Davidson VL. Use of the amicyanin signal sequence for efficient periplasmic expression in E. coli of a human antibody light chain variable domain. Protein Expression and Purification. 108: 9-12. PMID 25573388 DOI: 10.1016/J.Pep.2014.12.017 |
0.323 |
|
| 2015 |
Chacón-Verdú MD, Campillo-Brocal JC, Lucas-Elío P, Davidson VL, Sánchez-Amat A. Characterization of recombinant biosynthetic precursors of the cysteine tryptophylquinone cofactors of l-lysine-epsilon-oxidase and glycine oxidase from Marinomonas mediterranea. Biochimica Et Biophysica Acta. 1854: 1123-31. PMID 25542375 DOI: 10.1016/J.Bbapap.2014.12.018 |
0.461 |
|
| 2014 |
Williamson HR, Dow BA, Davidson VL. Mechanisms for control of biological electron transfer reactions. Bioorganic Chemistry. 57: 213-21. PMID 25085775 DOI: 10.1016/J.Bioorg.2014.06.006 |
0.723 |
|
| 2014 |
Shin S, Choi M, Williamson HR, Davidson VL. A simple method to engineer a protein-derived redox cofactor for catalysis. Biochimica Et Biophysica Acta. 1837: 1595-601. PMID 24858537 DOI: 10.1016/J.Bbabio.2014.05.354 |
0.789 |
|
| 2014 |
Dow BA, Sukumar N, Matos JO, Choi M, Schulte A, Tatulian SA, Davidson VL. The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Archives of Biochemistry and Biophysics. 550: 20-7. PMID 24704124 DOI: 10.1016/J.Abb.2014.03.010 |
0.635 |
|
| 2014 |
Shin S, Yukl ET, Sehanobish E, Wilmot CM, Davidson VL. Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG. Biochemistry. 53: 1342-9. PMID 24517455 DOI: 10.1021/Bi5000349 |
0.689 |
|
| 2014 |
Sehanobish E, Shin S, Sanchez-Amat A, Davidson VL. Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase. Febs Letters. 588: 752-6. PMID 24462691 DOI: 10.1016/J.Febslet.2014.01.021 |
0.663 |
|
| 2014 |
Shin S, Davidson VL. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Archives of Biochemistry and Biophysics. 544: 112-8. PMID 24144526 DOI: 10.1016/J.Abb.2013.10.004 |
0.718 |
|
| 2014 |
Wilmot C, Yukl E, Jensen L, Davidson V. MauG catalysis: a tale of ferryl iron, radicals and long distance hopping Acta Crystallographica Section a Foundations and Advances. 70: C312-C312. DOI: 10.1107/S2053273314096879 |
0.45 |
|
| 2013 |
Yukl ET, Williamson HR, Higgins L, Davidson VL, Wilmot CM. Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways. Biochemistry. 52: 9447-55. PMID 24320950 DOI: 10.1021/Bi401441H |
0.754 |
|
| 2013 |
Shin S, Feng M, Davidson VL. Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis. The Biochemical Journal. 456: 129-37. PMID 24024544 DOI: 10.1042/Bj20130981 |
0.657 |
|
| 2013 |
Abu Tarboush N, Yukl ET, Shin S, Feng M, Wilmot CM, Davidson VL. Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG. Biochemistry. 52: 6358-67. PMID 23952537 DOI: 10.1021/Bi400905S |
0.656 |
|
| 2013 |
Yukl ET, Jensen LM, Davidson VL, Wilmot CM. Structures of MauG in complex with quinol and quinone MADH. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 69: 738-43. PMID 23832199 DOI: 10.1107/S1744309113016539 |
0.311 |
|
| 2013 |
Davidson VL, Wilmot CM. Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. Annual Review of Biochemistry. 82: 531-50. PMID 23746262 DOI: 10.1146/Annurev-Biochem-051110-133601 |
0.505 |
|
| 2013 |
Geng J, Dornevil K, Davidson VL, Liu A. Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG. Proceedings of the National Academy of Sciences of the United States of America. 110: 9639-44. PMID 23720312 DOI: 10.1073/Pnas.1301544110 |
0.405 |
|
| 2013 |
Abu Tarboush N, Jensen LM, Wilmot CM, Davidson VL. A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis. Febs Letters. 587: 1736-41. PMID 23669364 DOI: 10.1016/J.Febslet.2013.04.047 |
0.452 |
|
| 2013 |
Yukl ET, Liu F, Krzystek J, Shin S, Jensen LM, Davidson VL, Wilmot CM, Liu A. Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 110: 4569-73. PMID 23487750 DOI: 10.1073/Pnas.1215011110 |
0.698 |
|
| 2012 |
Abu Tarboush N, Shin S, Geng J, Liu A, Davidson VL. Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity. Febs Letters. 586: 4339-43. PMID 23127557 DOI: 10.1016/J.Febslet.2012.10.044 |
0.646 |
|
| 2012 |
Jensen LM, Meharenna YT, Davidson VL, Poulos TL, Hedman B, Wilmot CM, Sarangi R. Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 1241-55. PMID 23053529 DOI: 10.1007/S00775-012-0939-3 |
0.363 |
|
| 2012 |
Choi M, Shin S, Davidson VL. Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex. Biochemistry. 51: 6942-9. PMID 22897160 DOI: 10.1021/Bi300817D |
0.763 |
|
| 2012 |
Chen Y, Naik SG, Krzystek J, Shin S, Nelson WH, Xue S, Yang JJ, Davidson VL, Liu A. Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG. Biochemistry. 51: 1586-97. PMID 22320333 DOI: 10.1021/Bi201575F |
0.62 |
|
| 2012 |
Davidson VL, Liu A. Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification. Biochimica Et Biophysica Acta. 1824: 1299-305. PMID 22314272 DOI: 10.1016/J.Bbapap.2012.01.008 |
0.517 |
|
| 2012 |
Feng M, Jensen LM, Yukl ET, Wei X, Liu A, Wilmot CM, Davidson VL. Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG. Biochemistry. 51: 1598-606. PMID 22299652 DOI: 10.1021/Bi201882E |
0.467 |
|
| 2011 |
Sukumar N, Choi M, Davidson VL. Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. Journal of Inorganic Biochemistry. 105: 1638-44. PMID 22071089 DOI: 10.1016/J.Jinorgbio.2011.08.002 |
0.63 |
|
| 2011 |
Tarboush NA, Jensen LM, Yukl ET, Geng J, Liu A, Wilmot CM, Davidson VL. Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 108: 16956-61. PMID 21969534 DOI: 10.1073/Pnas.1109423108 |
0.457 |
|
| 2011 |
Davidson VL. Ion-protein coordination: the many faces of a proton. Nature Chemistry. 3: 662-3. PMID 21860447 DOI: 10.1038/Nchem.1122 |
0.33 |
|
| 2011 |
Yukl ET, Goblirsch BR, Davidson VL, Wilmot CM. Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation. Biochemistry. 50: 2931-8. PMID 21355604 DOI: 10.1021/Bi200023N |
0.42 |
|
| 2011 |
Choi M, Sukumar N, Mathews FS, Liu A, Davidson VL. Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50: 1265-73. PMID 21268585 DOI: 10.1021/Bi101794Y |
0.682 |
|
| 2011 |
Choi M, Davidson VL. Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes. Metallomics : Integrated Biometal Science. 3: 140-51. PMID 21258692 DOI: 10.1039/C0Mt00061B |
0.634 |
|
| 2011 |
Shin S, Feng M, Chen Y, Jensen LM, Tachikawa H, Wilmot CM, Liu A, Davidson VL. The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis. Biochemistry. 50: 144-50. PMID 21128656 DOI: 10.1021/Bi101819M |
0.617 |
|
| 2011 |
Davidson VL. Generation of protein-derived redox cofactors by posttranslational modification. Molecular Biosystems. 7: 29-37. PMID 20936199 DOI: 10.1039/C005311B |
0.439 |
|
| 2011 |
Jensen L, Sanishvili R, Tarboush NA, Davidson V, Wilmot C. Protein complex structures inform about the reactivity of the hemoprotein MauG Acta Crystallographica Section a Foundations of Crystallography. 67: C218-C218. DOI: 10.1107/S0108767311094591 |
0.31 |
|
| 2010 |
Abu Tarboush N, Jensen LM, Feng M, Tachikawa H, Wilmot CM, Davidson VL. Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine . Biochemistry. 49: 9783-91. PMID 20929212 DOI: 10.1021/Bi101254P |
0.444 |
|
| 2010 |
Shin S, Abu Tarboush N, Davidson VL. Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase. Biochemistry. 49: 5810-6. PMID 20540536 DOI: 10.1021/Bi1004969 |
0.696 |
|
| 2010 |
Sukumar N, Mathews FS, Langan P, Davidson VL. A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer Proceedings of the National Academy of Sciences of the United States of America. 107: 6817-6822. PMID 20351252 DOI: 10.1073/Pnas.0912672107 |
0.395 |
|
| 2010 |
Jensen LM, Sanishvili R, Davidson VL, Wilmot CM. In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex. Science (New York, N.Y.). 327: 1392-4. PMID 20223990 DOI: 10.1126/Science.1182492 |
0.458 |
|
| 2009 |
Fu R, Liu F, Davidson VL, Liu A. Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands. Biochemistry. 48: 11603-5. PMID 19911786 DOI: 10.1021/Bi9017544 |
0.429 |
|
| 2009 |
Shin S, Lee S, Davidson VL. Suicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate. Biochemistry. 48: 10106-12. PMID 19788236 DOI: 10.1021/Bi901284E |
0.639 |
|
| 2009 |
Choi M, Sukumar N, Liu A, Davidson VL. Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48: 9174-84. PMID 19715303 DOI: 10.1021/Bi900836H |
0.661 |
|
| 2009 |
Wilmot CM, Davidson VL. Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis. Current Opinion in Chemical Biology. 13: 469-74. PMID 19648051 DOI: 10.1016/J.Cbpa.2009.06.026 |
0.45 |
|
| 2009 |
Lee S, Shin S, Li X, Davidson VL. Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 48: 2442-7. PMID 19196017 DOI: 10.1021/Bi802166C |
0.748 |
|
| 2008 |
Li X, Fu R, Lee S, Krebs C, Davidson VL, Liu A. A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical. Proceedings of the National Academy of Sciences of the United States of America. 105: 8597-600. PMID 18562294 DOI: 10.1073/Pnas.0801643105 |
0.593 |
|
| 2008 |
Davidson VL. Protein control of true, gated, and coupled electron transfer reactions. Accounts of Chemical Research. 41: 730-8. PMID 18442271 DOI: 10.1021/Ar700252C |
0.431 |
|
| 2008 |
Li X, Fu R, Liu A, Davidson VL. Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry. 47: 2908-12. PMID 18220357 DOI: 10.1021/Bi702259W |
0.636 |
|
| 2008 |
Ma JK, Lee S, Choi M, Bishop GR, Hosler JP, Davidson VL. The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin. Journal of Inorganic Biochemistry. 102: 342-6. PMID 17986390 DOI: 10.1016/J.Jinorgbio.2007.09.007 |
0.605 |
|
| 2007 |
Ma JK, Wang Y, Carrell CJ, Mathews FS, Davidson VL. A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin. Biochemistry. 46: 11137-46. PMID 17824674 DOI: 10.1021/Bi7012307 |
0.601 |
|
| 2007 |
Li T, Ma JK, Hosler JP, Davidson VL, Liu A. Detection of transient intermediates in the metal-dependent nonoxidative decarboxylation catalyzed by alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase. Journal of the American Chemical Society. 129: 9278-9. PMID 17625866 DOI: 10.1021/Ja073648L |
0.378 |
|
| 2007 |
Ma JK, Mathews FS, Davidson VL. Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energy. Biochemistry. 46: 8561-8. PMID 17602663 DOI: 10.1021/Bi700303E |
0.427 |
|
| 2007 |
Davidson VL. Protein-derived cofactors. Expanding the scope of post-translational modifications. Biochemistry. 46: 5283-92. PMID 17439161 DOI: 10.1021/Bi700468T |
0.404 |
|
| 2007 |
Carrell CJ, Ma JK, Antholine WE, Hosler JP, Mathews FS, Davidson VL. Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties. Biochemistry. 46: 1900-12. PMID 17295442 DOI: 10.1021/Bi0619674 |
0.392 |
|
| 2007 |
Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM. Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. Journal of Synchrotron Radiation. 14: 92-8. PMID 17211075 DOI: 10.1107/S0909049506051259 |
0.311 |
|
| 2006 |
Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 45: 13500-10. PMID 17087503 DOI: 10.1021/Bi0612972 |
0.405 |
|
| 2006 |
Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 13276-83. PMID 17073448 DOI: 10.1021/Bi061497D |
0.623 |
|
| 2006 |
Pearson AR, Marimanikkuppam S, Li X, Davidson VL, Wilmot CM. Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase. Journal of the American Chemical Society. 128: 12416-7. PMID 16984182 DOI: 10.1021/Ja064466E |
0.535 |
|
| 2006 |
Ma JK, Carrell CJ, Mathews FS, Davidson VL. Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated. Biochemistry. 45: 8284-93. PMID 16819827 DOI: 10.1021/Bi0605134 |
0.466 |
|
| 2006 |
Ono K, Okajima T, Tani M, Kuroda S, Sun D, Davidson VL, Tanizawa K. Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase. The Journal of Biological Chemistry. 281: 13672-84. PMID 16546999 DOI: 10.1074/Jbc.M600029200 |
0.566 |
|
| 2006 |
Li X, Feng M, Wang Y, Tachikawa H, Davidson VL. Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 821-8. PMID 16411758 DOI: 10.1021/Bi052000N |
0.664 |
|
| 2005 |
Ma JK, Bishop GR, Davidson VL. The ligand geometry of copper determines the stability of amicyanin. Archives of Biochemistry and Biophysics. 444: 27-33. PMID 16289023 DOI: 10.1016/J.Abb.2005.09.016 |
0.331 |
|
| 2005 |
Wang Y, Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. Journal of the American Chemical Society. 127: 8258-9. PMID 15941239 DOI: 10.1021/Ja051734K |
0.701 |
|
| 2005 |
Davidson VL. Structure and mechanism of tryptophylquinone enzymes. Bioorganic Chemistry. 33: 159-70. PMID 15888309 DOI: 10.1016/J.Bioorg.2004.10.001 |
0.49 |
|
| 2005 |
Sun D, Li X, Mathews FS, Davidson VL. Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled. Biochemistry. 44: 7200-6. PMID 15882058 DOI: 10.1021/Bi050288A |
0.689 |
|
| 2005 |
Jones LH, Pearson AR, Tang Y, Wilmot CM, Davidson VL. Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase. The Journal of Biological Chemistry. 280: 17392-6. PMID 15734739 DOI: 10.1074/Jbc.M500943200 |
0.434 |
|
| 2004 |
Carrell CJ, Wang X, Jones L, Jarrett WL, Davidson VL, Mathews FS. Crystallographic and NMR investigation of cobalt-substituted amicyanin. Biochemistry. 43: 9381-9. PMID 15260481 DOI: 10.1021/Bi049635R |
0.332 |
|
| 2004 |
Carrell CJ, Sun D, Jiang S, Davidson VL, Mathews FS. Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper. Biochemistry. 43: 9372-80. PMID 15260480 DOI: 10.1021/Bi049634Z |
0.557 |
|
| 2004 |
Davidson VL. Electron transfer in quinoproteins. Archives of Biochemistry and Biophysics. 428: 32-40. PMID 15234267 DOI: 10.1016/J.Abb.2004.03.022 |
0.473 |
|
| 2004 |
Pearson AR, De La Mora-Rey T, Graichen ME, Wang Y, Jones LH, Marimanikkupam S, Agger SA, Grimsrud PA, Davidson VL, Wilmot CM. Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation. Biochemistry. 43: 5494-502. PMID 15122915 DOI: 10.1021/Bi049863L |
0.593 |
|
| 2004 |
Ferrari D, Di Valentin M, Carbonera D, Merli A, Chen ZW, Mathews FS, Davidson VL, Rossi GL. Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 231-7. PMID 14735334 DOI: 10.1007/S00775-003-0513-0 |
0.394 |
|
| 2003 |
Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL. X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 843-54. PMID 14505072 DOI: 10.1007/S00775-003-0485-0 |
0.329 |
|
| 2003 |
Sun D, Ono K, Okajima T, Tanizawa K, Uchida M, Yamamoto Y, Mathews FS, Davidson VL. Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans. Biochemistry. 42: 10896-903. PMID 12974623 DOI: 10.1021/Bi035062R |
0.63 |
|
| 2003 |
Jones LH, Liu A, Davidson VL. An engineered CuA Amicyanin capable of intermolecular electron transfer reactions. The Journal of Biological Chemistry. 278: 47269-74. PMID 12970350 DOI: 10.1074/Jbc.M308863200 |
0.436 |
|
| 2003 |
Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM, Davidson VL. MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry. 42: 7318-25. PMID 12809487 DOI: 10.1021/Bi034243Q |
0.572 |
|
| 2003 |
Davidson VL. Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55. Biochimica Et Biophysica Acta. 1647: 230-3. PMID 12686138 DOI: 10.1016/S1570-9639(03)00056-6 |
0.342 |
|
| 2003 |
Pearson AR, Jones LH, Higgins L, Ashcroft AE, Wilmot CM, Davidson VL. Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation. Biochemistry. 42: 3224-30. PMID 12641453 DOI: 10.1021/Bi027073A |
0.357 |
|
| 2003 |
Davidson VL, Sun D. Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin. Journal of the American Chemical Society. 125: 3224-5. PMID 12630872 DOI: 10.1021/Ja0297133 |
0.612 |
|
| 2003 |
Sun D, Davidson VL. Effects of engineering uphill electron transfer into the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex. Biochemistry. 42: 1772-6. PMID 12578392 DOI: 10.1021/Bi0271594 |
0.61 |
|
| 2002 |
Davidson VL. Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer. Biochemistry. 41: 14633-6. PMID 12475211 DOI: 10.1021/Bi026812K |
0.39 |
|
| 2002 |
Sun D, Chen ZW, Mathews FS, Davidson VL. Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin. Biochemistry. 41: 13926-33. PMID 12437349 DOI: 10.1021/Bi026654X |
0.583 |
|
| 2002 |
Sun D, Wang X, Davidson VL. Redox properties of an engineered purple Cu(A) azurin. Archives of Biochemistry and Biophysics. 404: 158-62. PMID 12127080 DOI: 10.1016/S0003-9861(02)00282-5 |
0.524 |
|
| 2002 |
Davidson VL, Sun D. Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria. Methods in Enzymology. 353: 121-30. PMID 12078488 DOI: 10.1016/S0076-6879(02)53042-1 |
0.465 |
|
| 2002 |
Sun D, Davidson VL. Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55. Febs Letters. 517: 172-4. PMID 12062431 DOI: 10.1016/S0014-5793(02)02615-7 |
0.542 |
|
| 2002 |
Bao L, Sun D, Tachikawa H, Davidson VL. Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenase. Analytical Chemistry. 74: 1144-8. PMID 11924976 DOI: 10.1021/Ac0106086 |
0.487 |
|
| 2002 |
Wang Y, Sun D, Davidson VL. Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase. The Journal of Biological Chemistry. 277: 4119-22. PMID 11733518 DOI: 10.1074/Jbc.M109270200 |
0.669 |
|
| 2002 |
Sun D, Davidson VL. Mechanisms of catalysis and electron transfer by tryptophan tryptophylquinone enzymes Progress in Reaction Kinetics and Mechanism. 27: 209-241. DOI: 10.3184/007967402103165397 |
0.597 |
|
| 2001 |
Sun D, Jones LH, Mathews FS, Davidson VL. Active-site residues are critical for the folding and stability of methylamine dehydrogenase. Protein Engineering. 14: 675-81. PMID 11707614 DOI: 10.1093/Protein/14.9.675 |
0.569 |
|
| 2001 |
Davidson VL. Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase Advances in Protein Chemistry. 58: 95-140. PMID 11665494 DOI: 10.1016/S0065-3233(01)58003-1 |
0.44 |
|
| 2001 |
Sun D, Davidson VL. Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer. Biochemistry. 40: 12285-91. PMID 11591147 DOI: 10.1021/Bi011246Z |
0.597 |
|
| 2000 |
Davidson VL. Methylamine dehydrogenase. Structure and function of electron transfer complexes Sub-Cellular Biochemistry. 35: 119-143. PMID 11192720 DOI: 10.1007/0-306-46828-X_4 |
0.346 |
|
| 2000 |
Zhu Z, Sun D, Davidson VL. Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue. Biochemistry. 39: 11184-6. PMID 10985763 DOI: 10.1021/Bi001568N |
0.583 |
|
| 2000 |
Davidson VL. Effects of kinetic coupling on experimentally determined electron transfer parameters Biochemistry. 39: 4924-4928. PMID 10769151 DOI: 10.1021/Bi992671J |
0.343 |
|
| 2000 |
Davidson VL. Structure, function, and applications of tryptophan tryptophylquinone enzymes Advances in Experimental Medicine and Biology. 467: 587-595. PMID 10721104 DOI: 10.1007/978-1-4615-4709-9_73 |
0.495 |
|
| 2000 |
Davidson VL, Jones LH, Graichen ME, Zhu Z. Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathways. Biochimica Et Biophysica Acta. 1457: 27-35. PMID 10692547 DOI: 10.1016/S0005-2728(00)00052-9 |
0.4 |
|
| 2000 |
Davidson VL. What controls the rates of interprotein electron-transfer reactions Accounts of Chemical Research. 33: 87-93. PMID 10673316 DOI: 10.1021/Ar9900616 |
0.398 |
|
| 2000 |
Singh V, Zhu Z, Davidson VL, McCracken J. Characterization of the tryptophan tryptophyl-semiquinone catalytic intermediate of methylamine dehydrogenase by electron spin-echo envelope modulation spectroscopy Journal of the American Chemical Society. 122: 931-938. DOI: 10.1021/Ja9934246 |
0.394 |
|
| 2000 |
Davidson VL, Zhu Z. Reaction products and intermediates of tryptophan tryptophylquinone enzymes Journal of Molecular Catalysis - B Enzymatic. 8: 69-83. DOI: 10.1016/S1381-1177(99)00069-7 |
0.483 |
|
| 1999 |
Zhu Z, Sun D, Davidson VL. Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria. Journal of Bacteriology. 181: 6540-2. PMID 10515948 DOI: 10.1128/Jb.181.20.6540-6542.1999 |
0.519 |
|
| 1999 |
Hyun YL, Zhu Z, Davidson VL. Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin Journal of Biological Chemistry. 274: 29081-29086. PMID 10506161 DOI: 10.1074/Jbc.274.41.29081 |
0.409 |
|
| 1999 |
Graichen ME, Jones LH, Sharma BV, van Spanning RJ, Hosler JP, Davidson VL. Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides. Journal of Bacteriology. 181: 4216-22. PMID 10400578 DOI: 10.1128/Jb.181.14.4216-4222.1999 |
0.308 |
|
| 1999 |
Zhu Z, Davidson VL. Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin Biochemistry. 38: 4862-4867. PMID 10200175 DOI: 10.1021/Bi982939R |
0.421 |
|
| 1999 |
Davidson VL. Methylamine dehydrogenase: Structure and function of electron transfer complexes Biochemical Society Transactions. 27: 201-206. PMID 10093734 DOI: 10.1042/Bst0270201 |
0.346 |
|
| 1998 |
Zhu Z, Cunane LM, Chen ZW, Durley RCE, Mathews FS, Davidson VL. Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin Biochemistry. 37: 17128-17136. PMID 9860825 DOI: 10.1021/Bi9817919 |
0.393 |
|
| 1998 |
Zhu Z, Davidson VL. Methylamine dehydrogenase is a light-dependent oxidase Biochimica Et Biophysica Acta - Bioenergetics. 1364: 297-300. PMID 9630684 DOI: 10.1016/S0005-2728(98)00035-8 |
0.344 |
|
| 1998 |
Zhu Z, Davidson VL. Redox properties of tryptophan tryptophylquinone enzymes: Correlation with structure and reactivity Journal of Biological Chemistry. 273: 14254-14260. PMID 9603931 DOI: 10.1074/Jbc.273.23.14254 |
0.452 |
|
| 1998 |
Davidson VL, Jones LH, Zhu Z. Site-directed mutagenesis of Phe 97 to Glu in amicyanin alters the electronic coupling for interprotein electron transfer from quinol methylamine dehydrogenase. Biochemistry. 37: 7371-7. PMID 9585551 DOI: 10.1021/Bi973020V |
0.46 |
|
| 1998 |
Chen L, Doi M, Durley RCE, Chistoserdov AY, Lidstrom ME, Davidson VL, Mathews FS. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 Å resolution Journal of Molecular Biology. 276: 131-149. PMID 9514722 DOI: 10.1006/Jmbi.1997.1511 |
0.393 |
|
| 1998 |
Bishop GR, Zhu Z, Whitehead TL, Hicks RP, Davidson VL. Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR Biochemical Journal. 330: 1159-1163. PMID 9494080 DOI: 10.1042/Bj3301159 |
0.354 |
|
| 1997 |
Bishop GR, Davidson VL. Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction Biochemistry. 36: 13586-13592. PMID 9354627 DOI: 10.1021/bi970586a |
0.313 |
|
| 1997 |
Davidson VL, Jones LH, Graichen ME, Mathews FS, Hosler JP. Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis. Biochemistry. 36: 12733-8. PMID 9335529 DOI: 10.1021/Bi971353M |
0.412 |
|
| 1996 |
Davidson VL. Unraveling the kinetic complexity of interprotein electron transfer reactions. Biochemistry. 35: 14035-9. PMID 8916887 DOI: 10.1021/Bi961577P |
0.382 |
|
| 1996 |
Falzon L, Davidson VL. Intramolecular electron transfer in trimethylamine dehydrogenase: A thermodynamic analysis Biochemistry. 35: 12111-12118. PMID 8810917 DOI: 10.1021/Bi960664E |
0.445 |
|
| 1996 |
Davidson VL, Jones LH. Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex. Biochemistry. 35: 8120-5. PMID 8679563 DOI: 10.1021/Bi952854F |
0.428 |
|
| 1996 |
Falzon L, Davidson VL. Kinetic model for the regulation by substrate of intramolecular electron transfer in trimethylamine dehydrogenase Biochemistry. 35: 2445-2452. PMID 8652588 DOI: 10.1021/Bi951550Q |
0.445 |
|
| 1996 |
Merli A, Brodersen DE, Morini B, Chen ZW, Durley RCE, Mathews FS, Davidson VL, Rossi GL. Enzymatic and electron transfer activities in crystalline protein complexes Journal of Biological Chemistry. 271: 9177-9180. PMID 8621571 DOI: 10.1074/Jbc.271.16.9177 |
0.437 |
|
| 1996 |
Bishop GR, Valente EJ, Whitehead TL, Brown KL, Hicks RP, Davidson VL. Direct detection by 15N NMR of the tryptophan tryptophylquinone aminoquinol reaction intermediate of methylamine dehydrogenase Journal of the American Chemical Society. 118: 12868-12869. DOI: 10.1021/Ja9621859 |
0.309 |
|
| 1996 |
Falzon L, Davidson VL. Regulation of electron transfer in trimethylamine dehydrogenase by substrate Faseb Journal. 10. |
0.326 |
|
| 1996 |
Falzon L, Davidson VL. Regulation of electron transfer in trjmethylamine dehydrogenase by substrate Faseb Journal. 10. |
0.325 |
|
| 1996 |
Bishop GR, Davidson VL. Reaction intermediates and mechanisms for the oxidation of MADH byamicyanin Faseb Journal. 10. |
0.337 |
|
| 1996 |
Bishop GR, Davidson VL. Reaction intermediates and mechanisms for the oxidation of MADH by amicyanin Faseb Journal. 10. |
0.332 |
|
| 1995 |
Davidson VL, Brooks HB, Graichen ME, Jones LH, Hyun YL. Detection of intermediates in tryptophan tryptophylquinone enzymes. Methods in Enzymology. 258: 176-90. PMID 8524149 DOI: 10.1016/0076-6879(95)58046-8 |
0.336 |
|
| 1995 |
Edwards SL, Davidson VL, Hyun YL, Wingfield PT. Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes Journal of Biological Chemistry. 270: 4293-4298. PMID 7876189 DOI: 10.1074/Jbc.270.9.4293 |
0.458 |
|
| 1995 |
Davidson VL, Jones LH. Roles of dipolar effects and local charge in the ionic strength dependence of redox reactions between c-type cytochromes. Biochemistry. 34: 1238-43. PMID 7827073 DOI: 10.1021/Bi00004A017 |
0.354 |
|
| 1995 |
Hyun YL, Davidson VL. Mechanistic studies of aromatic amine dehydrogenase, a tryptophan tryptophylquinone enzyme. Biochemistry. 34: 816-23. PMID 7827040 DOI: 10.1021/Bi00003A015 |
0.45 |
|
| 1995 |
Davidson VL, Graichen ME, Jones LH. Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase. The Biochemical Journal. 308: 487-92. PMID 7772031 DOI: 10.1042/Bj3080487 |
0.404 |
|
| 1995 |
Hyun YL, Davidson VL. Unusually large isotope effect for the reaction of aromatic amine dehydrogenase. A common feature of quinoproteins? Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1251: 198-200. PMID 7669810 DOI: 10.1016/0167-4838(95)00117-D |
0.419 |
|
| 1995 |
Loughran MG, Hall JM, Turner AP, Davidson VL. Amperometric detection of histamine at a quinoprotein dehydrogenase enzyme electrode. Biosensors & Bioelectronics. 10: 569-76. PMID 7612208 DOI: 10.1016/0956-5663(95)96932-O |
0.312 |
|
| 1995 |
Davidson VL, Jones LH. Complex formation with methylamine dehydrogenase affects the pathway of electron transfer from amicyanin to cytochrome c-551i. The Journal of Biological Chemistry. 270: 23941-3. PMID 7592588 DOI: 10.1074/Jbc.270.41.23941 |
0.409 |
|
| 1995 |
Davidson VL, Jones LH. Reaction mechanism for the inactivation of the quinoprotein methylamine dehydrogenase by phenylhydrazine. Biochimica Et Biophysica Acta. 1252: 146-50. PMID 7548156 DOI: 10.1016/0167-4838(95)00114-A |
0.417 |
|
| 1995 |
Hyun YL, Davidson VL. Electron transfer reactions between aromatic amine dehydrogenase and azurin Biochemistry. 34: 12249-12254. PMID 7547967 DOI: 10.1021/Bi00038A020 |
0.467 |
|
| 1995 |
Bishop GR, Davidson VL. Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer Biochemistry. 34: 12082-12086. PMID 7547947 DOI: 10.1021/bi00037a052 |
0.328 |
|
| 1995 |
Warncke K, Brooks HB, Lee HI, McCracken J, Davidson VL, Babcock GT. Structure of the dithionite-generated tryptophan tryptophylquinone cofactor radical in methylamine dehydrogenase revealed by ENDOR and ESEEM spectroscopies Journal of the American Chemical Society. 117: 10063-10075. DOI: 10.1021/Ja00145A018 |
0.343 |
|
| 1994 |
Harris TK, Davidson VL. Replacement of enzyme-bound calcium with strontium alters the kinetic properties of methanol dehydrogenase Biochemical Journal. 300: 175-182. PMID 8198531 DOI: 10.1042/Bj3000175 |
0.356 |
|
| 1994 |
Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. Journal of Bacteriology. 176: 2922-9. PMID 8188594 DOI: 10.1128/Jb.176.10.2922-2929.1994 |
0.382 |
|
| 1994 |
Brooks HB, Davidson VL. Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin Biochemistry. 33: 5696-5701. PMID 8180195 DOI: 10.1021/Bi00185A005 |
0.412 |
|
| 1994 |
Chen L, Durley RCE, Mathews FS, Davidson VL. Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin, and cytochrome c551i Science. 264: 86-90. PMID 8140419 DOI: 10.1126/Science.8140419 |
0.422 |
|
| 1994 |
Harris TK, Davidson VL. Thermal stability of methanol dehydrogenase is altered by the replacement of enzyme-bound Ca2+ with Sr2+ Biochemical Journal. 303: 141-145. PMID 7945232 DOI: 10.1042/Bj3030141 |
0.342 |
|
| 1994 |
Davidson VL. Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: evidence of conformationally coupled electron transfer Biochemistry®. 33: 12600-12608. PMID 7918485 DOI: 10.1021/Bi00208A010 |
0.442 |
|
| 1994 |
Brooks HB, Davidson VL. Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin Journal of the American Chemical Society. 116: 11201-11202. DOI: 10.1021/Ja00103A063 |
0.359 |
|
| 1993 |
Durley R, Chen L, Lim LW, Mathews FS, Davidson VL. Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 Å and 1.8 Å resolution Protein Science. 2: 739-752. PMID 8495197 DOI: 10.1002/Pro.5560020506 |
0.347 |
|
| 1993 |
Brooks HB, Jones LH, Davidson VL. Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase. Biochemistry. 32: 2725-9. PMID 8448129 DOI: 10.1021/Bi00061A034 |
0.36 |
|
| 1993 |
Harris TK, Davidson VL. A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus denitrificans Biochemistry. 32: 4362-4368. PMID 8386543 DOI: 10.1021/Bi00067A028 |
0.429 |
|
| 1993 |
Chen L, Mathews FS, Davidson VL, Tegoni M, Rivetti C, Rossi GL. Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome Protein Science. 2: 147-154. PMID 8382992 DOI: 10.1002/Pro.5560020203 |
0.389 |
|
| 1993 |
Brooks HB, Davidson VL. A method for extracting rate constants from initial rates of stopped-flow kinetic data: Application to a physiological electron-transfer reaction Biochemical Journal. 294: 211-213. PMID 8363574 DOI: 10.1042/Bj2940211 |
0.407 |
|
| 1993 |
Davidson VL, Graichen ME, Jones LH. Binding constants for a physiologic electron-transfer protein complex between methylamine dehydrogenase and amicyanin. Effects of ionic strength and bound copper on binding. Biochimica Et Biophysica Acta. 1144: 39-45. PMID 8347660 DOI: 10.1016/0005-2728(93)90028-E |
0.412 |
|
| 1993 |
Harris TK, Davidson VL. Binding and electron transfer reactions between methanol dehydrogenase and its physiologic electron acceptor cytochrome c-551i: A kinetic and thermodynamic analysis Biochemistry. 32: 14145-14150. PMID 8260498 DOI: 10.1021/Bi00214A011 |
0.419 |
|
| 1993 |
White S, Boyd G, Mathews FS, Xia ZX, Dai WW, Zhang YF, Davidson VL. The active site structure of the calcium-containing quinoprotein methanol dehydrogenase Biochemistry. 32: 12955-12958. PMID 8241148 DOI: 10.1021/Bi00211A002 |
0.42 |
|
| 1993 |
Warncke K, Brooks HB, Babcock GT, Davidson VL, McCracken J. The nitrogen atom of substrate methylamine is incorporated into the tryptophan tryptophyl-semiquinone catalytic intermediate in methylamine dehydrogenase Journal of the American Chemical Society. 115: 6464-6465. DOI: 10.1021/Ja00067A093 |
0.315 |
|
| 1992 |
Davidson VL, Jones LH. Cofactor-directed inactivation by nucleophilic amines of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans. Biochimica Et Biophysica Acta. 1121: 104-10. PMID 1599932 DOI: 10.1016/0167-4838(92)90343-C |
0.431 |
|
| 1992 |
Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FMD, Hol WGJ. Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin Biochemistry. 31: 4959-4964. PMID 1599920 DOI: 10.1021/Bi00136A006 |
0.372 |
|
| 1992 |
Davidson VL, Jones LH, Graichen ME. Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins. Biochemistry. 31: 3385-90. PMID 1554720 |
0.308 |
|
| 1992 |
Chen L, Mathews FS, Davidson VL, Huizinga EG, Vellieux FMD, Hol WGJ. Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 Å resolution Proteins: Structure, Function and Genetics. 14: 288-299. PMID 1409575 DOI: 10.1002/Prot.340140214 |
0.327 |
|
| 1992 |
Davidson VL, Wu J, Miller B, Jones LH. Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans. Fems Microbiology Letters. 73: 53-8. PMID 1325939 DOI: 10.1111/J.1574-6968.1992.Tb05288.X |
0.327 |
|
| 1992 |
Davidson VL, Kumar MA, Wu J. Apparent oxygen-dependent inhibition by superoxide dismutase of the quinoprotein methanol dehydrogenase Biochemistry®. 31: 1504-1508. PMID 1310612 DOI: 10.1021/Bi00120A030 |
0.403 |
|
| 1991 |
Davidson VL, Jones LH. Inhibition by cyclopropylamine of the quinoprotein methylamine dehydrogenase is mechanism-based and causes covalent cross-linking of alpha and beta subunits. Biochemistry. 30: 1924-8. PMID 1993204 DOI: 10.1021/Bi00221A027 |
0.383 |
|
| 1991 |
Backes G, Davidson VL, Huitema F, Duine JA, Sanders-Loehr J. Characterization of the tryptophan-derived quinone cofactor of methylamine dehydrogenase by resonance Raman spectroscopy. Biochemistry. 30: 9201-10. PMID 1892829 DOI: 10.1021/Bi00102A011 |
0.327 |
|
| 1991 |
Chen L, Mathews FS, Davidson VL, Huizinga EG, Vellieux FMD, Duine JA, Hol WGJ. Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase Febs Letters. 287: 163-166. PMID 1879526 DOI: 10.1016/0014-5793(91)80041-Z |
0.313 |
|
| 1991 |
Davidson VL, Jones LH. Intermolecular electron transfer from quinoproteins and its relevance to biosensor technology Analytica Chimica Acta. 249: 235-240. DOI: 10.1016/0003-2670(91)87028-6 |
0.418 |
|
| 1990 |
Kumar MA, Davidson VL. Chemical cross-linking study of complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. Biochemistry. 29: 5299-304. PMID 2383547 DOI: 10.1021/Bi00474A012 |
0.362 |
|
| 1990 |
Davidson VL, Kumar MA. Inhibition by trimethylamine of methylamine oxidation by Paracoccus denitrificans and bacterium W3A1 Bba - Bioenergetics. 1016: 339-343. PMID 2331476 DOI: 10.1016/0005-2728(90)90166-2 |
0.347 |
|
| 1990 |
Davidson VL, Jones LH, Kumar MA. pH-dependent semiquinone formation by methylamine dehydrogenase from Paracoccus denitrificans. Evidence for intermolecular electron transfer between quinone cofactors. Biochemistry. 29: 10786-91. PMID 2271681 DOI: 10.1021/Bi00500A010 |
0.413 |
|
| 1989 |
Davidson VL. Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans Biochemical Journal. 261: 107-111. PMID 2775197 DOI: 10.1042/Bj2610107 |
0.394 |
|
| 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 |
0.395 |
|
| 1989 |
Davidson VL, Kumar MA. Cytochrome c-550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans Febs Letters. 245: 271-273. PMID 2538362 DOI: 10.1016/0014-5793(89)80235-2 |
0.309 |
|
| 1988 |
Gray KA, Davidson VL, Knaff DB. Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans Journal of Biological Chemistry. 263: 13987-13990. PMID 3170535 |
0.341 |
|
| 1987 |
Husain M, Davidson VL, Gray KA, Knaff DB. Redox properties of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans Biochemistry. 26: 4139-4143. PMID 3651442 DOI: 10.1021/Bi00387A059 |
0.42 |
|
| 1987 |
Husain M, Davidson VL. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans Journal of Bacteriology. 169: 1712-1717. PMID 3558322 DOI: 10.1128/Jb.169.4.1712-1717.1987 |
0.391 |
|
| 1987 |
Davidson VL, Neher JW. Evidence for two subclasses of methylamine dehydrogenases with distinct large subunits and conserved PQQ-bearing small subunits Fems Microbiology Letters. 44: 121-124. DOI: 10.1111/J.1574-6968.1987.Tb02254.X |
0.35 |
|
| 1986 |
Davidson VL, Husain M, Neher JW. Electron transfer flavoprotein from Methylophilus methylotrophus: Properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source Journal of Bacteriology. 166: 812-817. PMID 3711024 DOI: 10.1128/Jb.166.3.812-817.1986 |
0.363 |
|
| 1986 |
Gray KA, Knaff DB, Husain M, Davidson VL. Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans Febs Letters. 207: 239-242. PMID 3021532 DOI: 10.1016/0014-5793(86)81496-X |
0.317 |
|
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