Cytochrome c nitrite reductase: from structural to physicochemical analysis

Burlat, B., Gwyer, J. D., Poock, S., Clarke, T. A. ORCID: https://orcid.org/0000-0002-6234-1914, Cole, J. A., Hemmings, A. M., Cheesman, M. R., Butt, J. N. ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 (2005) Cytochrome c nitrite reductase: from structural to physicochemical analysis. Biochemical Society Transactions, 33 (1). pp. 137-140. ISSN 1470-8752

Full text not available from this repository. (Request a copy)

Abstract

The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Energy Materials Laboratory (former - to 2025) Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes (former - to 2025) Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Chemistry of Light and Energy (former - to 2025) Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Wolfson Centre for Advanced Environmental Microbiology Faculty of Science > Research Groups > Pharmacology and Biological Chemistry
Depositing User:	Users 2731 not found.
Date Deposited:	24 May 2011 10:24
Last Modified:	18 Jun 2026 15:35
URI:	https://ueaeprints.uea.ac.uk/id/eprint/31294
DOI:	10.1042/BST0330137

Actions (login required)

View Item