Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity.
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Turnover-Dependent Covalent Inactivation of Staphylococcus aureus Coenzyme A-Disulfide Reductase by Coenzyme A-Mimetics: Mechanistic and Structural Insights1,4-naphthoquinones and other NADPH-dependent glutathione reductase-catalyzed redox cyclers as antimalarial agentsAnalytical methods for kinetic studies of biological interactions: A reviewTight-binding inhibitors efficiently inactivate both reaction centers of monomeric Plasmodium falciparum glyoxalase 1.Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for Catalytically Competent Nitroreductase.
P2860
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity.
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2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@ast
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@en
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi
@nl
type
label
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@ast
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@en
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi
@nl
prefLabel
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@ast
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@en
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi
@nl
P2860
P356
P1433
P1476
Reduction kinetics of a flavin ...... (TH1): half-sites reactivity.
@en
P2093
David P Ballou
Sarayut Nijvipakul
P2860
P304
P356
10.1021/BI1009985
P407
P577
2010-11-01T00:00:00Z