Regulation of the H+/e− stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios

Frank, Viola; Kadenbach, Bernhard

doi:10.1016/0014-5793(96)00096-8

Cited by 112 publications

(110 citation statements)

References 18 publications

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“…Inhibition of cytochrome-c oxidase activity by ATP was shown by Ferguson-Miller et al (1976) using Keilin-Hartree particles. Binding of ATP to the N-terminal domain of subunit VIaH (Anthony et al, 1993) reduces the efficiency of proton pumping (H +/e-stoichiometry) of the reconstituted enzyme from bovine heart by 50% (Frank and Kadenbach, 1996). Cytochrome-c oxidase from bovine heart contains seven high-affinity binding sites for ATP and ten for ADP, as shown by equilibrium dialysis with the labelled nucleotides (Napiwotzki et al, 1997).…”

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confidence: 99%

Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐c Oxidase

Arnold¹,

Kadenbach²

1997

European Journal of Biochemistry

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212

184

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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‐c‐binding sites in the dimeric enzyme complex is mediated by cardiolipin, which is essential for cooperativity of the enzyme within the lipid membrane.

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mentioning

confidence: 99%

Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐c Oxidase

Arnold¹,

Kadenbach²

1997

European Journal of Biochemistry

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212

184

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“…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). On isolated mitochondria, the occurrence of such changes in H C pumping ef ciency (i.e., redox slipping) may depend on several parameters, that is, the size of the protonmotive force, the kinetic constraints in electron delivery to the respiratory chain, and the relative contribution of COX to the control of respiration.…”

Section: Discussionmentioning

confidence: 99%

“…It is worth noting that this ATPinduced decrease in H C pumping stoichiometry seems to be rather speci c to the subunit VIa-H expression, because it was not observed in bovine liver, in turkey liver, and in turkey heart (16,27). Ratio (see also Table 2)…”

Section: Effect Of Extra-and Intraliposomal Adenylic Nucleotides On Kmentioning

confidence: 92%

“…By comparing measurements performed under coupling and uncoupling conditions, it was shown that intramatricial ADP, in contrast to ATP, increases the respiratory control ratio, thereby suggesting that H C pumping is affected by intraliposomal adenylic nucleotides (45). Furthermore, a decrease in the H C /e ¡ stoichiometry at high intraliposomal ATP/ADP ratios was nally observed by direct measurements of H C translocation (16,27).…”

Section: Effect Of Extra-and Intraliposomal Adenylic Nucleotides On Kmentioning

confidence: 96%

“…Cytochrome c oxidase (COX), which catalyzes one of the irreversible steps of the energy-transduction pathway, has been shown to be a controlling step in rat liver (4), rat heart (6), and yeast (7) mitochondria. Moreover, numerous studies emphasize the potential regulatory properties of this enzyme, and some show that the stoichiometry of the proton pumping, which was originally assumed to be 1 H C per e ¡ , is variable and dependent on many parameters (8)(9)(10)(11)(12)(13)(14)(15) including allosteric regulations (16). Of course, the rate of electron transfer through cytochrome oxidase is controlled by the associated thermodynamic forces: a) the span in redox potential between oxygen and cytochrome c (i.e., 1E h ) and b) the proton electrochemical potential difference.…”

Section: Introductionmentioning

confidence: 99%

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Regulation of Cytochrome c Oxidase by Adenylic Nucleotides. Is Oxidative Phosphorylation Feedback Regulated by its End‐Products?

Beauvoit¹,

Rigoulet²

2001

IUBMB Life

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SummaryCytochrome c oxidase, which catalyzes an irreversible step of the respiratory chain, is one of the rate-controlling steps of oxidative phosphorylation on isolated mitochondria. The rate of electron transfer through the complex is primarily controlled by the associated thermodynamic forces, i.e., the span in redox potential between oxygen and cytochrome c and the protonmotive force. However, the electron ux also depends on the various kinetic effectors, including adenylic nucleotides. Although the number of binding sites for ATP and ADP on cytochrome oxidase is still a matter of debate, experiments performed on the solubilized and reconstituted enzyme provide strong functional evidence that the mammalian cytochrome c oxidase binds adenylic nucleotides on both sides of the inner membrane. These effects include modi cation in cytochrome c af nity, allosteric inhibition and changes in proton pumping ef ciency. Immunological studies have pointed out the role of subunit IV and that of an ATP-binding protein, subunit VIa, in these kinetic regulations. In yeast, the role of the nuclear-encoded subunits in assembly and regulation of the cytochrome c oxidase has been further substantiated by using gene-disruption analysis. Using a subunit VIa-null mutant, the consequences of the ATP regulation on oxidative phosphorylation have been further investigated on isolated mitochondria. Taken together, the data demonstrate that there are multiple regulating sites for ATP on the yeast cytochrome oxidase with respect to the location (matrix versus cytosolic side), kinetic effect (activation versus inhibition) and consequence on the ow-force relationships. The question is therefore raised as to the

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Mitochondrial Cytochrome c Oxidase

Shinzawa‐Itoh¹,

Yamashita²,

Tsukihara³

2004

Handbook of Metalloproteins

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Cytochrome c oxidase reduces molecular oxygen (O 2 ) to water (coupled with proton pumping) at its O 2 reduction site composed of an iron ion (heme a 3 ) and a copper ion (Cu B ) by electrons transferred from cytochrome c in the intermembrane space by Cu A and heme a in the enzyme protein and by protons from the matrix space. Mitochondrial cytochrome c oxidase, isolated from bovine heart muscle as early as in 1941, was crystallized to determine the X‐ray structure at 2.3/2.35 Å resolutions in the fully oxidized/reduced states in 1998, showing 13 different subunits and Cu B , liganded with three histidine imidazole groups in a trigonal‐planer coordination in the fully reduced state. A tyrosine phenol group is fixed close to the O 2 reduction site with a covalent link with one of the three imidazole groups. This O 2 reduction site structure suggests that Fe a 3 O 2 and Fe a 3 OOH are stable and unstable, respectively, to form FeO as the second intermediate in the O 2 reduction process, consistent with the resonance Raman results for the process. A fairly big redox‐coupled X‐ray structural change in an aspartate (Asp51) located near the intermembrane surface of the enzyme molecule suggesting a large redox‐coupled pKa change in Asp51 and a hydrogen bond network connecting Asp51 with the matrix surface indicate that Asp51 is the site for proton pumping. A peptide bond in the hydrogen bond network facilitates the unidirectional proton transfer through the hydrogen bond network up to Asp51.

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Regulation of the H⁺/e⁻ stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios

Cited by 112 publications

References 18 publications

Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐c Oxidase

Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐c Oxidase

Regulation of Cytochrome c Oxidase by Adenylic Nucleotides. Is Oxidative Phosphorylation Feedback Regulated by its End‐Products?

Mitochondrial Cytochrome c Oxidase

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