The Inhibition of Glutathione Reductase by Quinones

Abstract 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 μᴍ and uncompetitive in­ hibitors for gluta...

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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-1991-9-1042
https://www.degruyter.com/view/journals/znc/46/9-10/article-p966.xml
https://www.degruyter.com/document/doi/10.1515/znc-1991-9-1042/pdf
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Summary:Abstract 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 μᴍ and uncompetitive in­ hibitors 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 inter­ face 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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