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Mitochondrial F-type ATP synthase: multiple enzyme functions revealed by the membrane-embedded F O structure.
- Source :
-
Critical reviews in biochemistry and molecular biology [Crit Rev Biochem Mol Biol] 2020 Aug; Vol. 55 (4), pp. 309-321. Date of Electronic Publication: 2020 Jun 24. - Publication Year :
- 2020
-
Abstract
- Of the two main sectors of the F-type ATP synthase, the membrane-intrinsic F <subscript>O</subscript> domain is the one which, during evolution, has undergone the highest structural variations and changes in subunit composition. The F <subscript>O</subscript> complexity in mitochondria is apparently related to additional enzyme functions that lack in bacterial and thylakoid complexes. Indeed, the F-type ATP synthase has the main bioenergetic role to synthesize ATP by exploiting the electrochemical gradient built by respiratory complexes. The F <subscript>O</subscript> membrane domain, essential in the enzyme machinery, also participates in the bioenergetic cost of synthesizing ATP and in the formation of the cristae , thus contributing to mitochondrial morphology. The recent enzyme involvement in a high-conductance channel, which forms in the inner mitochondrial membrane and promotes the mitochondrial permeability transition, highlights a new F-type ATP synthase role. Point mutations which cause amino acid substitutions in F <subscript>O</subscript> subunits produce mitochondrial dysfunctions and lead to severe pathologies. The F <subscript>O</subscript> variability in different species, pointed out by cryo-EM analysis, mirrors the multiple enzyme functions and opens a new scenario in mitochondrial biology.
Details
- Language :
- English
- ISSN :
- 1549-7798
- Volume :
- 55
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Critical reviews in biochemistry and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 32580582
- Full Text :
- https://doi.org/10.1080/10409238.2020.1784084