Abstract
The protein complexes of the mitochondrial oxidative phosphorylation system were recently reported to form supramolecular assemblies termed respiratory supercomplexes or respirasomes. These supercomplexes are considered to be of great functional importance. Here we review new insights into supercomplex structure and physiology.
Highlights
The protein complexes of the mitochondrial oxidative phosphorylation system were recently reported to form supramolecular assemblies termed respiratory supercomplexes or respirasomes
Electron transfer is mediated by a number of prosthetic groups and co-factors attached to defined subunits of the four oxidoreductase complexes: 2Fe-2S clusters, 4Fe-4S clusters, heme groups of the a, b, and c type, a flavine mononucleotide, and copper atoms
The oxidative phosphorylation (OXPHOS)2 system forms the basis for mitochondrial ATP production
Summary
The oxidative phosphorylation (OXPHOS) system forms the basis for mitochondrial ATP production In most organisms it is composed of the ATP synthase complex (complex V) and four oxidoreductase complexes: the NADH dehydrogenase (complex I), the succinate dehydrogenase (complex II), the cytochrome c reductase (complex III), and the cytochrome c oxidase (complex IV). Complex III transfers electrons from ubiquinol to cytochrome c This small protein is localized in the space between the outer and inner mitochondrial membrane. The alternative oxidoreductases do not couple electron transport with proton translocation across the inner mitochondrial membrane These enzymes are considered to form the basis of an overflow protection mechanism for the respiratory chain under certain physiological conditions, e.g. high light conditions in plants
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