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Exploring the conformational equilibrium of E. coli thioredoxin reductase: Characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy

The conformational dynamics of wild-type Escherichia coli thioredoxin reductase (TrxR) and the mutant enzyme C138S were studied by ultrafast time-resolved fluorescence of the flavin cofactor in combination with circular dichroism (both in the flavin fingerprint and far-UV regions) and steady-state f...

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Detalhes bibliográficos
Main Authors: Van Den Berg, Petra A.W., Mulrooney, Scott B., Gobets, Bas, Van Stokkum, Ivo H.M., Van Hoek, Arie, Williams, Charles H., Visser, Antonie J.W.G.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 2001
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2374229/
https://ncbi.nlm.nih.gov/pubmed/11567095
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