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Lookup NU author(s): Professor Christopher Dennison
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Copper is widely used in nature to promote electron transfer in a variety of processes. The metal is usually found as a mononuclear type 1 copper site protected by a protein envelope, which has become known as a cupredoxin fold. In the past few years, the use of protein engineering combined with various spectroscopic and kinetic approaches has provided detailed information about cupredoxins and cupredoxin domains. This review will describe some of the recent advances that have been made, highlighting that there is still a long way to go before we fully appreciate the complexity of biological electron transfer proteins. © 2005 Elsevier B.V. All rights reserved.
Author(s): Dennison C
Publication type: Review
Publication status: Published
Journal: Coordination Chemistry Reviews
Year: 2005
Volume: 249
Issue: 24
Pages: 3025-3054
Print publication date: 15/12/2005
ISSN (print): 0010-8545
ISSN (electronic): 1873-3840
URL: http://dx.doi.org/10.1016/j.ccr.2005.04.021
DOI: 10.1016/j.ccr.2005.04.021
