The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones

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.

Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (55 K)Download as PowerPoint slideHighlights► The coordination chemistry of cuprous copper shows remarkable plasticity. ► Cuprous ions can deform and reorganize with remarkably low energies. ► The plasticity of the cuprous oxidation state may enable transport.