Magnetic circular dichroism evidence for a weakly coupled heme-radical pair at the active site of cytochrome cd(1), a nitrite reductase

Oganesyan, Vasily ORCID: https://orcid.org/0000-0002-8738-1146, Cheesman, M. R. and Thomson, Andrew (2007) Magnetic circular dichroism evidence for a weakly coupled heme-radical pair at the active site of cytochrome cd(1), a nitrite reductase. Inorganic Chemistry, 46 (26). pp. 10950-10952. ISSN 0020-1669

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Abstract

In nitrite-treated cytochrome cd(1) nitrite reductase, heme d(1) is electron paramagnetic resonance silent but paramagnetic. Analysis of the unusual temperature dependence of the magnetic circular dichroism spectra unambiguously demonstrates that the heme d(1) is not in the oxoferryl (Fe-IV=O) state but is low-spin Fe-III weakly coupled to a radical species. This species could be either a protein-bound radical generated by a nitrite ion reacting with a heme group resulting in a one-electron oxidation of an amino acid residue, possibly tyrosine or tryptophan, adjacent to heme d(1) or a heme d(1) (FeNO)-N-III complex.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry
Depositing User:	Rachel Smith
Date Deposited:	10 May 2011 10:12
Last Modified:	09 Feb 2023 13:36
URI:	https://ueaeprints.uea.ac.uk/id/eprint/30094
DOI:	10.1021/ic701556y

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