Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence

FEBS Letters

de Kok, A.¹  Visser, A.J.W.G.¹ 

[1] Department of Biochemistry, Agricultural University, 6703 BC Wageningen, The Netherlands

关键词: Glutathione reductase;    Lipoamide dehydrogenase;    Fluorescence anisotropy;    Rotational correlation time;    Flavin-binding site;    Flexibility;   

DOI  :  10.1016/0014-5793(87)81033-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown