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Biochim Biophys Acta. 2014 Apr;1837(4):418-26. doi: 10.1016/j.bbabio.2013.10.004. Epub 2013 Oct 30.

Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation.

Author information

1
Institute of Structural and Molecular Biology, Malet street, Birkbeck College, London WC1E 7HX, UK.
2
Electron Microscopy Group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747AG Groningen, The Netherlands.
3
Electron Microscopy Group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747AG Groningen, The Netherlands. Electronic address: n.dudkina@mail.cryst.bbk.ac.uk.

Abstract

Oxidative phosphorylation (OXPHOS) is the main source of energy in eukaryotic cells. This process is performed by means of electron flow between four enzymes, of which three are proton pumps, in the inner mitochondrial membrane. The energy accumulated in the proton gradient over the inner membrane is utilized for ATP synthesis by a fifth OXPHOS complex, ATP synthase. Four of the OXPHOS protein complexes associate into stable entities called respiratory supercomplexes. This review summarises the current view on the arrangement of the electron transport chain in mitochondrial cristae. The functional role of the supramolecular organisation of the OXPHOS system and the factors that stabilise such organisation are highlighted. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.

KEYWORDS:

ATP synthase; Electron microscopy; Mitochondria; Oxidative phosphorylation; Supercomplex

PMID:
24183696
DOI:
10.1016/j.bbabio.2013.10.004
[Indexed for MEDLINE]
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