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V L Davidson

Showing results (51-60 of 89) with videos related to

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Biochemistry|April 7, 1992
Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteinsV L Davidson, L H Jones, M E Graichen
Biochemistry|July 9, 1996
Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyaninG R Bishop, H B Brooks, V L Davidson
Biochemistry|March 16, 1993
Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenaseH B Brooks, L H Jones, V L Davidson
The Journal of Biological Chemistry|October 5, 1988
Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificansK A Gray, V L Davidson, D B Knaff
Proceedings of the National Academy of Sciences of the United States of America|March 31, 2010
A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transferN Sukumar, F S Mathews, P Langan, et al.
FEMS Microbiology Letters|July 1, 1992
Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificansV L Davidson, J Wu, B Miller, et al.
Biochemistry|July 29, 2000
Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridgeZ Zhu, L H Jones, M E Graichen, et al.
Biochimica Et Biophysica Acta|February 29, 2000
Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathwaysV L Davidson, L H Jones, M E Graichen, et al.
Protein Engineering|November 15, 2001
Active-site residues are critical for the folding and stability of methylamine dehydrogenaseD Sun, L H Jones, F S Mathews, et al.
Science (New York, N.Y.)|April 1, 1994
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551iL Chen, R C Durley, F S Mathews, et al.
Pageof 9

Showing results (51-60 of 89) with videos related to

Sort By:
Pageof 9
Biochemistry|April 7, 1992
Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteinsV L Davidson, L H Jones, M E Graichen
Biochemistry|July 9, 1996
Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyaninG R Bishop, H B Brooks, V L Davidson
Biochemistry|March 16, 1993
Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenaseH B Brooks, L H Jones, V L Davidson
The Journal of Biological Chemistry|October 5, 1988
Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificansK A Gray, V L Davidson, D B Knaff
Proceedings of the National Academy of Sciences of the United States of America|March 31, 2010
A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transferN Sukumar, F S Mathews, P Langan, et al.
FEMS Microbiology Letters|July 1, 1992
Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificansV L Davidson, J Wu, B Miller, et al.
Biochemistry|July 29, 2000
Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridgeZ Zhu, L H Jones, M E Graichen, et al.
Biochimica Et Biophysica Acta|February 29, 2000
Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathwaysV L Davidson, L H Jones, M E Graichen, et al.
Protein Engineering|November 15, 2001
Active-site residues are critical for the folding and stability of methylamine dehydrogenaseD Sun, L H Jones, F S Mathews, et al.
Science (New York, N.Y.)|April 1, 1994
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551iL Chen, R C Durley, F S Mathews, et al.
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