Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria. J Bioenerg Biomembr 2008 Oct;40(5):411-7
Date
10/08/2008Pubmed ID
18839289DOI
10.1007/s10863-008-9168-4Scopus ID
2-s2.0-57049106773 (requires institutional sign-in at Scopus site) 85 CitationsAbstract
Accumulating evidence indicates that the enzymes involved in mitochondrial oxidative phosphorylation (OXPHOS) are co-assembled into higher-ordered supercomplexes within the mitochondrial inner membrane. This review will focus largely on the OXPHOS supercomplexes of the yeast Saccharomyces cerevisiae. The recent evidence to indicate that diversity in the populations of the cytochrome bc (1)-COX supercomplexes exist shall be outlined. In addition, the existence of dimeric/oligomeric F(1)F(o)-ATP synthase complexes and their proposed role in establishment of the cristae architecture of the inner mitochondrial membrane shall also be discussed.
Author List
Stuart RAAuthor
Rosemary Stuart PhD Professor in the Biology department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
Electron Transport Chain Complex ProteinsElectron Transport Complex I
Electron Transport Complex III
Electron Transport Complex IV
Intracellular Membranes
Mitochondria
Mitochondrial Proton-Translocating ATPases
Models, Biological
Models, Molecular
Oxidative Phosphorylation
Saccharomyces cerevisiae
