Literature DB >> 21624365

Allosteric nucleotide-binding site in the mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I).

Vera G Grivennikova1, Grigory V Gladyshev, Andrei D Vinogradov.   

Abstract

The rotenone-insensitive NADH:hexaammineruthenium III (HAR) oxidoreductase reactions catalyzed by bovine heart and Yarrowia lipolytica submitochondrial particles or purified bovine complex I are stimulated by ATP and other purine nucleotides. The soluble fraction of mammalian complex I (FP) and prokaryotic complex I homolog NDH-1 in Paracoccus denitrificans plasma membrane lack stimulation of their activities by ATP. The stimulation appears as a decrease in apparent K(m) values for NADH and HAR. Thus, the "accessory" subunits of eukaryotic complex I bear an allosteric ATP-binding site.
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2011        PMID： 21624365      PMCID： PMC3138810          DOI： 10.1016/j.febslet.2011.05.039

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  46 in total

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Journal:  FEBS Lett       Date:  1991-07-29       Impact factor: 4.124

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  2 in total

1.  Cellular Compartmentation and the Redox/Nonredox Functions of NAD.

Authors:  Chaitanya A Kulkarni; Paul S Brookes
Journal:  Antioxid Redox Signal       Date:  2019-03-26       Impact factor: 8.401

2.  Nucleoside reverse transcriptase inhibitors induce a mitophagy-associated endothelial cytotoxicity that is reversed by coenzyme Q10 cotreatment.

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Journal:  Toxicol Sci       Date:  2013-05-02       Impact factor: 4.849
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