Reversible dimerization of cytochrome c oxidase regulates mitochondrial respiration
| Autor: | Sebastian Vogt, Bernhard Kadenbach, Petra Weber, Rabia Ramzan, Annika Rhiel |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Male Allosteric regulation Respiratory chain Oxidative phosphorylation Mitochondrion Crystallography X-Ray Calcium in biology Electron Transport Complex IV Mitochondrial Proteins 03 medical and health sciences 0302 clinical medicine Oxygen Consumption Allosteric Regulation Respiration Cytochrome c oxidase Inner membrane Animals Rats Wistar Molecular Biology biology Chemistry Cell Biology Rats 030104 developmental biology Biophysics biology.protein Molecular Medicine Protein Multimerization 030217 neurology & neurosurgery |
| Zdroj: | Mitochondrion. 49 |
| ISSN: | 1872-8278 |
| Popis: | Almost all energy consumed by higher organisms, either in the form of ATP or heat, is produced in mitochondria by respiration and oxidative phosphorylation through five protein complexes in the inner membrane. High-resolution x-ray analysis of crystallized cytochrome c oxidase (CytOx), the final oxygen-accepting complex of the respiratory chain, isolated by using cholate as detergent, revealed a dimeric structure with 13 subunits in each monomer. In contrast, CytOx isolated with non-ionic detergents appeared to be monomeric. Our data indicate in vivo a continuous transition between CytOx monomers and dimers via reversible phosphorylation. Increased intracellular calcium, as a consequence of stress, dephosphorylates and monomerises CytOx, whereas cAMP rephosphorylates and dimerises it. Only dimeric CytOx exhibits an "allosteric ATP-inhibition" which inhibits respiration at high cellular ATP/ADP-ratios and could prevent oxygen radical formation and the generation of diseases. |
| Databáze: | OpenAIRE |
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