title: The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones.
abstract: Copper plays vital roles in the active sites of cytochrome oxidase and in several other enzymes essential for human health. Copper is also highly toxic when dysregulated; because of this an elaborate array of accessory proteins have evolved which act as intracellular carriers or chaperones for the copper ions. In most cases chaperones transport cuprous copper. This review discusses some of the chemistry of these copper sites, with a view to some of the structural factors in copper coordination which are important in the biological function of these chaperones. The coordination chemistry and accessible geometries of the cuprous oxidation state are remarkably plastic and we discuss how this may relate to biological function. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes.
authors: Department of Geological Sciences, University of Saskatchewan, Saskatoon, SK, Canada S7N5E2.
authors: M Jake
authors: MJ
authors: Pushie
authors: Limei
authors: L
authors: Zhang
authors: Ingrid J
authors: IJ
authors: Pickering
authors: Graham N
authors: GN
authors: George
mesh_terms: D000465:Algorithms; D000818:Animals; D003067:Coenzymes / Q000737:chemistry; D056831:Coordination Complexes / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000096:biosynthesis; D005583:Fourier Analysis; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D013816:Thermodynamics; D056928:X-Ray Absorption Spectroscopy
chemical_list: D003067:Coenzymes; D056831:Coordination Complexes; D018832:Molecular Chaperones; D013438:Sulfhydryl Compounds; D003300:Copper; D003576:Electron Transport Complex IV