title: Copper trafficking to the mitochondrion and assembly of copper metalloenzymes.
abstract: Copper is required within the mitochondrion for the function of two metalloenzymes, cytochrome c oxidase (CcO) and superoxide dismutase (Sod1). Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space and is mediated by metallochaperone proteins. Cox17 is a key copper donor to two accessory proteins, Sco1 and Cox11, to form the two copper centers in the mature CcO complex. Ccs1 is the necessary metallochaperone for the copper metallation of Sod1 in the IMS as well as within the cytoplasm where the bulk of Sod1 resides. Copper ions used in the metallation of CcO and Sod1 appear to be provided by a novel copper pool within the mitochondrial matrix. This review documents copper ion shuttling within the mitochondrion and the proteins that mediate assembly of active CcO and Sod1.
authors.affiliation: Departments of Medicine and Biochemistry, University of Utah Health Sciences Center, Salt Lake City, UT 84132, USA.
authors.forename: Paul A
authors.initials: PA
authors.lastname: Cobine
authors.forename: Fabien
authors.initials: F
authors.lastname: Pierrel
authors.forename: Dennis R
authors.initials: DR
authors.lastname: Winge
mesh_terms: D001692:Biological Transport; D003300:Copper / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D003300:Copper; D003576:Electron Transport Complex IV