Flavin Binding Site Differences Between Lipoamide Dehydrogenase and Glutathione Reductase As Revealed by Static and Time-resolved Flavin Fluorescence

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 1987 Jun 22

PMID 3595857

Citations 5

Authors

A de Kok

A J Visser

Affiliations

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Abstract

Subnanosecond-resolved fluorescence measurements of the FAD bound in glutathione reductase and lipoamide dehydrogenase revealed characteristic differences in dynamic properties of both enzymes, which are considered to have common structural features. The flavin fluorescence in glutathione reductase is quenched mainly via a dynamic mechanism, in agreement with enhanced flexibility of the flavin as inferred from rapid depolarization of the fluorescence.

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