Cholate Disrupts Regulatory Functions of Cytochrome c Oxidase.
ATP binding site
allosteric ATP-Inhibition
cholat
cytochrome c oxidase
regulatory function
Journal
Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052
Informations de publication
Date de publication:
23 06 2021
23 06 2021
Historique:
received:
24
02
2021
revised:
10
06
2021
accepted:
17
06
2021
entrez:
2
7
2021
pubmed:
3
7
2021
medline:
27
10
2021
Statut:
epublish
Résumé
Cytochrome c oxidase (CytOx), the oxygen-accepting and rate-limiting enzyme of mitochondrial respiration, binds with 10 molecules of ADP, 7 of which are exchanged by ATP at high ATP/ADP-ratios. These bound ATP and ADP can be exchanged by cholate, which is generally used for the purification of CytOx. Many crystal structures of isolated CytOx were performed with the enzyme isolated from mitochondria using sodium cholate as a detergent. Cholate, however, dimerizes the enzyme isolated in non-ionic detergents and induces a structural change as evident from a spectral change. Consequently, it turns off the "allosteric ATP-inhibition of CytOx", which is reversibly switched on under relaxed conditions via cAMP-dependent phosphorylation and keeps the membrane potential and ROS formation in mitochondria at low levels. This cholate effect gives an insight into the structural-functional relationship of the enzyme with respect to ATP inhibition and its role in mitochondrial respiration and energy production.
Identifiants
pubmed: 34201437
pii: cells10071579
doi: 10.3390/cells10071579
pmc: PMC8303988
pii:
doi:
Substances chimiques
Cholates
0
Adenosine Diphosphate
61D2G4IYVH
Electron Transport Complex IV
EC 1.9.3.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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