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Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase

Item Type:Article
Title:Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase
Creators Name:Arnold, S. and Kadenbach, B.
Abstract:The activity of cytochrome-c oxidase, the terminal enzyme of the mitochondrial respiratory chain, is known to be regulated by the substrate pressure, i.e. the ferro-/ferricytochrome c ratio, by the oxygen concentration, and by the electrochemical proton gradient delta muH+ across the inner mitochondrial membrane. Here we describe a further mechanism of 'respiratory control' via allosteric inhibition of cytochrome-c oxidase by ATP, which binds to the matrix domain, of subunit IV. The cooperativity between cytochrome-c-binding sites in the dimeric enzyme complex is mediated by cardiolipin, which is essential for cooperativity of the enzyme within the lipid membrane.
Keywords:Cytochrome-C Oxidase, Allosteric Enzyme, ATP/ADP Ratio, Hill Coefficient, Cardiolipin
Source:European Journal of Biochemistry
ISSN:0014-2956
Publisher:Blackwell Publishing (U.K.)
Volume:249
Number:1
Page Range:350-354
Date:1 October 1997
Official Publication:https://doi.org/10.1111/j.1432-1033.1997.t01-1-00350.x
PubMed:View item in PubMed

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