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Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.

Thioredoxin reductase (TrxR) from Escherichia coli consists of two globular domains connected by a two-stranded beta sheet: an FAD domain and a pyridine nucleotide binding domain. The latter domain contains the redox-active disulfide composed of Cys 135 and Cys 138. TrxR is proposed to undergo a con...

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Enregistré dans:
Détails bibliographiques
Auteurs principaux: Mulrooney, S. B., Williams, C. H.
Format: Artigo
Langue:Inglês
Publié: Cold Spring Harbor Laboratory Press 1997
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143557/
https://ncbi.nlm.nih.gov/pubmed/9336841
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