Redox-triggered events in cytochrome c nitrite reductase

Gwyer, J, Angove, H, Richardson, D.J. and Butt, Julea (2004) Redox-triggered events in cytochrome c nitrite reductase. Bioelectrochemistry, 63 (1-2). pp. 43-47. ISSN 1878-562X

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Abstract

Escherichia coli cytochrome c nitrite reductase is a homodimeric enzyme whose 10 heme centres range in reduction potential from ca. -30 to -320 mV. Protein film voltammetry (PFV) was performed to assess how the reactivity of the enzyme towards a number of small molecules was influenced by heme oxidation state. The experimental approach provided a high-resolution description of activity across the electrochemical potential domain by virtue of the fact that the enzyme sample was under the precise potential control of an electrode at all times. The current potential profiles displayed by nitrite reductase revealed that heme oxidation state has a profound, and often unanticipated, effect on the interactions with substrate molecules, nitrite and hydroxylamine, as well as the inhibitor, cyanide. Thus, PFV provides a powerful route to define redox-triggered events in this complex multi-centred redox enzyme.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Science > School of Biological Sciences
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Depositing User: Rachel Smith
Date Deposited: 17 Feb 2011 12:12
Last Modified: 11 Apr 2019 14:44
URI: https://ueaeprints.uea.ac.uk/id/eprint/21416
DOI: 10.1016/j.bioelechem.2003.10.013

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