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...
Published in: | Zeitschrift für Naturforschung C |
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Walter de Gruyter GmbH
1991
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crdegruyter:10.1515/znc-1991-11-1207 2023-05-15T15:52:34+02:00 The Inhibition of Glutathione Reductase by Quinones Bironaitė, Daiva A. Čėnas, Narimantas K. Kulys, Juozas J. Medentsev, Alexander G. Akimenko, Vasiliy K. 1991 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 unknown Walter de Gruyter GmbH http://creativecommons.org/licenses/by-nc-nd/3.0/ CC-BY-NC-ND Zeitschrift für Naturforschung C volume 46, issue 11-12, page 966-968 ISSN 1865-7125 0939-5075 General Biochemistry, Genetics and Molecular Biology journal-article 1991 crdegruyter https://doi.org/10.1515/znc-1991-11-1207 2022-04-14T05:01:56Z 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. Article in Journal/Newspaper Carbonic acid De Gruyter (via Crossref) Zeitschrift für Naturforschung C 46 11-12 966 968 |
institution |
Open Polar |
collection |
De Gruyter (via Crossref) |
op_collection_id |
crdegruyter |
language |
unknown |
topic |
General Biochemistry, Genetics and Molecular Biology |
spellingShingle |
General Biochemistry, Genetics and Molecular Biology Bironaitė, Daiva A. Čėnas, Narimantas K. Kulys, Juozas J. Medentsev, Alexander G. Akimenko, Vasiliy K. The Inhibition of Glutathione Reductase by Quinones |
topic_facet |
General Biochemistry, Genetics and Molecular Biology |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Bironaitė, Daiva A. Čėnas, Narimantas K. Kulys, Juozas J. Medentsev, Alexander G. Akimenko, Vasiliy K. |
author_facet |
Bironaitė, Daiva A. Čėnas, Narimantas K. Kulys, Juozas J. Medentsev, Alexander G. Akimenko, Vasiliy K. |
author_sort |
Bironaitė, Daiva A. |
title |
The Inhibition of Glutathione Reductase by Quinones |
title_short |
The Inhibition of Glutathione Reductase by Quinones |
title_full |
The Inhibition of Glutathione Reductase by Quinones |
title_fullStr |
The Inhibition of Glutathione Reductase by Quinones |
title_full_unstemmed |
The Inhibition of Glutathione Reductase by Quinones |
title_sort |
inhibition of glutathione reductase by quinones |
publisher |
Walter de Gruyter GmbH |
publishDate |
1991 |
url |
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 |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_source |
Zeitschrift für Naturforschung C volume 46, issue 11-12, page 966-968 ISSN 1865-7125 0939-5075 |
op_rights |
http://creativecommons.org/licenses/by-nc-nd/3.0/ |
op_rightsnorm |
CC-BY-NC-ND |
op_doi |
https://doi.org/10.1515/znc-1991-11-1207 |
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Zeitschrift für Naturforschung C |
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46 |
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11-12 |
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966 |
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968 |
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1766387705462128640 |