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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Bibliographic Details
Main Authors: van den Berg, P A, van Hoek, A, Walentas, C D, Perham, R N, Visser, A J
Format: Artigo
Language:Inglês
Published: 1998
Subjects:
Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1299545/
https://ncbi.nlm.nih.gov/pubmed/9545063
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