Tools
Tools
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
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 (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) 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 > Centre for Photonics and Quantum Science |
| Depositing User: | Rachel Smith |
| Date Deposited: | 10 May 2011 10:12 |
| Last Modified: | 24 Sep 2024 09:43 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/30094 |
| DOI: | 10.1021/ic701556y |
Actions (login required)
 |
View Item |