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...
Published in: | Zeitschrift für Naturforschung C |
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Main Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
Walter de Gruyter GmbH
1991
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Subjects: | |
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 |
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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