Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase.
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Asymmetric Reduction of Activated Alkenes by Pentaerythritol Tetranitrate Reductase: Specificity and Control of Stereochemical Outcome by Reaction Optimisation.Probing active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed 'deep' H-tunnelling reactionBetter than Nature: Nicotinamide Biomimetics That Outperform Natural CoenzymesProbing the NADH- and Methyl Red-binding site of a FMN-dependent azoreductase (AzoA) from Enterococcus faecalis.Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for Catalytically Competent Nitroreductase.Drug design based on pentaerythritol tetranitrate reductase: synthesis and antibacterial activity of Pogostone derivatives.
P2860
Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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name
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@en
Bipartite recognition and conf ...... hritol tetranitrate reductase.
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type
label
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@en
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@nl
prefLabel
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@en
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@nl
P2860
P1433
P1476
Bipartite recognition and conf ...... hritol tetranitrate reductase.
@en
P2093
Nigel S Scrutton
P2860
P304
P356
10.1111/J.1742-4658.2009.07179.X
P407
P577
2009-07-31T00:00:00Z