Redox-triggered events in cytochrome c nitrite reductase

Gwyer, J, Angove, H, Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea ORCID: https://orcid.org/0000-0002-9624-5226 (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
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User:	Rachel Smith
Date Deposited:	17 Feb 2011 12:12
Last Modified:	16 May 2023 07:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21416
DOI:	10.1016/j.bioelechem.2003.10.013

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