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Victor L Davidson

Showing results (51-60 of 109) with videos related to

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Biochimica Et Biophysica Acta|May 27, 2014
A simple method to engineer a protein-derived redox cofactor for catalysisSooim Shin, Moonsung Choi, Heather R Williamson, et al.
FEBS Letters|May 10, 2017
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å awayManliang Feng, Zhongxin Ma, Breland F Crudup, et al.
Archives of Biochemistry and Biophysics|May 15, 2021
Diversity of structures and functions of oxo-bridged non-heme diiron proteinsMaria Luiza Caldas Nogueira, Anthony J Pastore, Victor L Davidson
FEBS Letters|January 28, 2014
Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidaseEsha Sehanobish, Sooim Shin, Antonio Sanchez-Amat, et al.
Biochemistry|November 20, 2002
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyaninDapeng Sun, Zhi-wei Chen, F Scott Mathews, et al.
Biochemistry|January 18, 2006
Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesisXianghui Li, Manliang Feng, Yongting Wang, et al.
The Journal of Biological Chemistry|October 17, 2019
Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidaseKyle J Mamounis, Dante Avalos, Erik T Yukl, et al.
Archives of Biochemistry and Biophysics|September 22, 2019
Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolaceaKyle J Mamounis, Zhongxin Ma, Antonio Sanchez-Amat, et al.
Science (New York, N.Y.)|March 13, 2010
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complexLyndal M R Jensen, Ruslan Sanishvili, Victor L Davidson, et al.
Biochemistry|January 28, 2011
Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interfaceMoonsung Choi, Narayanasami Sukumar, F Scott Mathews, et al.
Pageof 11

Showing results (51-60 of 109) with videos related to

Sort By:
Pageof 11
Biochimica Et Biophysica Acta|May 27, 2014
A simple method to engineer a protein-derived redox cofactor for catalysisSooim Shin, Moonsung Choi, Heather R Williamson, et al.
FEBS Letters|May 10, 2017
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å awayManliang Feng, Zhongxin Ma, Breland F Crudup, et al.
Archives of Biochemistry and Biophysics|May 15, 2021
Diversity of structures and functions of oxo-bridged non-heme diiron proteinsMaria Luiza Caldas Nogueira, Anthony J Pastore, Victor L Davidson
FEBS Letters|January 28, 2014
Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidaseEsha Sehanobish, Sooim Shin, Antonio Sanchez-Amat, et al.
Biochemistry|November 20, 2002
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyaninDapeng Sun, Zhi-wei Chen, F Scott Mathews, et al.
Biochemistry|January 18, 2006
Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesisXianghui Li, Manliang Feng, Yongting Wang, et al.
The Journal of Biological Chemistry|October 17, 2019
Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidaseKyle J Mamounis, Dante Avalos, Erik T Yukl, et al.
Archives of Biochemistry and Biophysics|September 22, 2019
Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolaceaKyle J Mamounis, Zhongxin Ma, Antonio Sanchez-Amat, et al.
Science (New York, N.Y.)|March 13, 2010
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complexLyndal M R Jensen, Ruslan Sanishvili, Victor L Davidson, et al.
Biochemistry|January 28, 2011
Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interfaceMoonsung Choi, Narayanasami Sukumar, F Scott Mathews, et al.
Pageof 11