Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.

Time-resolved polarized flavin fluorescence was used to study the active site dynamics of Escherichia coli glutathione reductase (GR). Special consideration was given to the role of Tyr177, which blocks the access to the NADPH binding-site in the crystal structure of the enzyme. By comparing wild-ty...

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Detaylı Bibliyografya
Asıl Yazarlar: van den Berg, P A, van Hoek, A, Walentas, C D, Perham, R N, Visser, A J
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1998
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1299545/
https://ncbi.nlm.nih.gov/pubmed/9545063
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