The Inhibition of Glutathione Reductase by Quinones

Fully substituted quinones including some naturally occurring oxyquinones acted as inhibitors of yeast glutathione reductase (EC 1.6.4.2). They were competitive, mixed or uncompetitive inhibitors for NADPH , possessing K i in the range of 1-200 μM and uncompetitive inhibitors for glutathione. Rhein...

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Bibliographic Details
Published in:Zeitschrift für Naturforschung C
Main Authors: Bironaitė, Daiva A., Čėnas, Narimantas K., Kulys, Juozas J., Medentsev, Alexander G., Akimenko, Vasiliy K.
Format: Article in Journal/Newspaper
Language:unknown
Published: Walter de Gruyter GmbH 1991
Subjects:
General Biochemistry, Genetics and Molecular Biology
Carbonic acid
Online Access:http://dx.doi.org/10.1515/znc-1991-11-1207
https://www.degruyter.com/view/journals/znc/46/11-12/article-p966.xml
https://www.degruyter.com/document/doi/10.1515/znc-1991-11-1207/pdf
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Summary:Fully substituted quinones including some naturally occurring oxyquinones acted as inhibitors of yeast glutathione reductase (EC 1.6.4.2). They were competitive, mixed or uncompetitive inhibitors for NADPH , possessing K i in the range of 1-200 μM and uncompetitive inhibitors for glutathione. Rhein (4,5-dioxy-9,10-anthraquinone- 2-carbonic acid) and 9,10-phenanthrenequinone were the most effective inhibitors. It is concluded that certain quinones can bind to the NADP(H )-binding site and to the heteroaromatics binding site at the interface domain (P. A. Karplus, E. F. Pai, and G. E. Schulz, Eur. J. Biochem. 178, 693-703 (1989)) of the enzyme.

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