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

M. Jake Pushie, Limei Zhang, Ingrid J. Pickering, Graham N. George

Research output: Contribution to journalReview article

20 Scopus citations

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 languageEnglish (US)
Pages (from-to)938-947
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1817
Issue number6
DOIs
StatePublished - Jun 2012

Keywords

  • Copper homeostasis
  • Copper transport
  • Cuprous thiolate clusters
  • EXAFS

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones'. Together they form a unique fingerprint.

  • Cite this