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The allosteric ATP‐inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP‐dependent phosphorylation

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Bender, Elisabeth, Kadenbach, Bernhard·2000·FEBS Letters

Abstract

In previous studies the allosteric inhibition of cytochrome c oxidase at high intramitochondrial ATP/ADP‐ratios via binding of the nucleotides to the matrix domain of subunit IV was demonstrated. Here we show that the allosteric ATP‐inhibition of the isolated bovine heart enzyme is switched on by cAMP‐dependent phosphorylation with protein kinase A of subunits II (and/or III) and Vb, and switched off by subsequent incubation with protein phosphatase 1. It is suggested that after cAMP‐dependent phosphorylation of cytochrome c oxidase mitochondrial respiration is controlled by the ATP/ADP‐ratio keeping the proton motive force Δ p low, and the efficiency of energy transduction high. After Ca 2+‐induced dephosphorylation this control is lost, accompanied by increase of Δ p, slip of proton pumping (decreased H+/e− stoichiometry), and increase of the rate of respiration and ATP‐synthesis at a decreased efficiency of energy transduction.

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Metadata

Authors
Bender, E., & Kadenbach, B.
Venue
FEBS Letters
Publisher
Wiley
Published
2000-01-18
Volume
466
Issue
1
Pages
130-134
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2050688382
Cited by
197
References
0
FWCI
3.38
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The allosteric ATP‐inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP‐dependent phosphorylation. https://app.cochat.ai/papers/10.1016/s0014-5793(99)01773-1
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Bender, E., & Kadenbach, B. (2000). The allosteric ATP‐inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP‐dependent phosphorylation. FEBS Letters. https://doi.org/10.1016/s0014-5793(99)01773-1

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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