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.
Original language | English (US) |
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Pages (from-to) | 938-947 |
Number of pages | 10 |
Journal | Biochimica et Biophysica Acta - Bioenergetics |
Volume | 1817 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2012 |
Externally published | Yes |
Keywords
- Copper homeostasis
- Copper transport
- Cuprous thiolate clusters
- EXAFS
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology