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- W2079492124 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." @default.
- W2079492124 created "2016-06-24" @default.
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- W2079492124 date "2012-06-01" @default.
- W2079492124 modified "2023-10-16" @default.
- W2079492124 title "The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones" @default.
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- W2079492124 doi "https://doi.org/10.1016/j.bbabio.2011.10.004" @default.
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