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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Allosteric Regulation*
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Animals
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Binding Sites
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Cattle
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Electron Transport Complex I / chemistry*
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Electron Transport Complex I / metabolism
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Fungal Proteins / chemistry*
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Fungal Proteins / metabolism
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Mitochondria / enzymology*
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NAD / metabolism
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NADH, NADPH Oxidoreductases / chemistry*
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NADH, NADPH Oxidoreductases / metabolism
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Nucleotides / metabolism*
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Paracoccus denitrificans / cytology
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Paracoccus denitrificans / metabolism
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Ruthenium Compounds / metabolism
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Yarrowia / cytology
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Yarrowia / metabolism
Substances
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Fungal Proteins
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Nucleotides
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Ruthenium Compounds
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NAD
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hexammineruthenium
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Adenosine Triphosphate
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NADH, NADPH Oxidoreductases
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Electron Transport Complex I