The Inhibition of Glutathione Reductase by Quinones
Open Access
- 1 October 1991
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 46 (9-10) , 966-968
- https://doi.org/10.1515/znc-1991-9-1042
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 Ki 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.Keywords
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