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BY-NC-ND 3.0 license Open Access Published by De Gruyter June 2, 2014

The Inhibition of Glutathione Reductase by Quinones

Daiva A. Bironaitė , Narimantas K. Čėnas , Juozas J. Kulys , Alexander G. Medentsev and Vasiliy K. Akimenko

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 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.

Received: 1991-3-4
Revised: 1991-5-7
Published Online: 2014-6-2
Published in Print: 1991-12-1

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