title: Sealing the mitochondrial respirasome.
abstract: The mitochondrial respiratory chain is organized within an array of supercomplexes that function to minimize the generation of reactive oxygen species (ROS) during electron transfer reactions. Structural models of supercomplexes are now known. Another recent advance is the discovery of non-OXPHOS complex proteins that appear to adhere to and seal the individual respiratory complexes to form stable assemblages that prevent electron leakage. This review highlights recent advances in our understanding of the structures of supercomplexes and the factors that mediate their stability.
authors.affiliation: University of Utah Health Sciences Center, Department of Medicine, Salt Lake City, Utah, USA. dennis.winge@hsc.utah.edu
authors.forename: Dennis R
authors.initials: DR
authors.lastname: Winge
mesh_terms: D000818:Animals; D004579:Electron Transport / Q000502:physiology*; D045222:Electron Transport Chain Complex Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D055503:Protein Multimerization; D017382:Reactive Oxygen Species / Q000378:metabolism
chemical_list: D045222:Electron Transport Chain Complex Proteins; D024101:Mitochondrial Proteins; D046912:Multiprotein Complexes; D017382:Reactive Oxygen Species