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Ligand and loop variations at type 1 copper sites: Influence on structure and reactivity

Lookup NU author(s): Professor Christopher Dennison

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Abstract

Type 1 (T1) copper sites promote biological electron transfer and are found in the cupredoxins and a number of copper-containing enzymes including the multi-copper oxidases. A T1 copper site usually has a distorted tetrahedral geometry with strong ligands provided by the thiolate sulfur of a Cys and the imidazole nitrogens of two His residues. The active site structure is typically completed by a weak axial Met ligand (a second weak axial interaction is found in azurin resulting in a trigonal bipyramidal geometry). The axial Met is not conserved and Gin, Phe, Leu and Val are also found in this position. Three of the four ligands at a T1 copper site are situated on a single C-terminal loop whose length and structure varies. Studies are discussed which investigate both the influence of physiologically relevant axial ligand alterations, and also of mutations to the length and structure of the ligand-containing loop, on the properties of T1 copper sites. © The Royal Society of Chemistry 2005.


Publication metadata

Author(s): Dennison C

Publication type: Review

Publication status: Published

Journal: Dalton Transactions

Year: 2005

Issue: 21

Pages: 3436-3442

ISSN (print): 1477-9226

ISSN (electronic): 1477-9234

URL: http://dx.doi.org/10.1039/b507440c

DOI: 10.1039/b507440c


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