1997
DOI: 10.1111/j.1432-1033.1997.t01-1-00350.x
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Abstract: The activity of cytochrome‐c oxidase, the terminal enzyme of the mitochondria) 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 ΔμH+ 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‐… Show more

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Cited by 200 publications
(186 citation statements)
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References 42 publications
(37 reference statements)
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“…In contrast to the external effect, the matrix-oriented inhibition of ATP is extensively documented in the literature for eucaryotic COX including yeast (80). There is strong evidence that this effect is linked to the cooperative binding of ferrocytochrome c to the dimeric enzyme, which can be abolished by decreasing the ATP/ADP (22,49,51,80). In addition to the effect on enzyme turnover, adenylic nucleotides seem to modulate the proton pumping ef ciency of isolated mammalian COX in a tissue-speci c manner (16,27).…”
Section: Discussionmentioning
confidence: 99%
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“…In contrast to the external effect, the matrix-oriented inhibition of ATP is extensively documented in the literature for eucaryotic COX including yeast (80). There is strong evidence that this effect is linked to the cooperative binding of ferrocytochrome c to the dimeric enzyme, which can be abolished by decreasing the ATP/ADP (22,49,51,80). In addition to the effect on enzyme turnover, adenylic nucleotides seem to modulate the proton pumping ef ciency of isolated mammalian COX in a tissue-speci c manner (16,27).…”
Section: Discussionmentioning
confidence: 99%
“…Hence, the sigmoidal substrate/activity relationship is a consequence of cooperative interaction between the two cytochrome c binding sites in the dimeric enzyme complex (i.e., Hill coef cient equals 2). Because cooperativity inevitably involves binding and dissociation of cytochrome c, it is lost when the COX activity is measured in the presence of TMPD as a direct electron donor to bound ferricytochrome c. Moreover, cooperativity is also lost when the enzyme is solubilized by dodecyl maltoside (49), which is known to monomerize the isolated enzyme and thus prevents cooperative interactions of the dimeric enzyme complex. Finally, the allosteric inhibition of the Tween 80-solubilized enzyme by ATP is abolished after preincubation with a monoclonal antibody against subunit IV (49).…”
Section: Allosteric Inhibition Of Cox By High Internal Atp/adpmentioning
confidence: 99%
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“…Arnold and Kadenbach have shown that high intramitochondrial ATP/ADP ratios convert the hyperbolic kinetics of ascorbate‐dependent respiration of isolated CytOx to an inhibited allosteric kinetic status (Hill coefficient >1), which is independent of the Ψm and is based on the binding of ATP or ADP to the matrix domain of CytOx subunit IV 72. Ogbi et al 73 observed that phosphorylation of CytOx subunit IV by protein kinase Cϵ produced an increase in the CytOx activity.…”
Section: Ros Have Double Functionsmentioning
confidence: 99%