Assignment of conformation-sensitive near-infrared bands in high-spin ferrous haemoproteins. Low-temperature magnetic circular dichroism data

Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146 and Sharonov, Yuri A. (1997) Assignment of conformation-sensitive near-infrared bands in high-spin ferrous haemoproteins. Low-temperature magnetic circular dichroism data. Theoretical Chemistry Accounts, 96 (4). pp. 261-268. ISSN 1432-881X

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Abstract

An assignment of the near-infrared bands in the 600-800 nm spectral region observed in magnetic circular dichroism (MCD) spectra of high-spin ferrous haemoproteins is presented. The assignment is based on a relative energy level scheme for iron d-electrons, a comparison of predicted and measured temperature dependences of MCD intensity, a sign of MCD bands and a group theoretical analysis of allowed transitions. The proposed assignment is consistent with the ∼15-nm red shift of the ∼760 nm band on breakage of the Fe-His bond in deoxy-myoglobin at low pH, with low-temperature photolysis experiments available for CO complexes of several haemoproteins. In accordance with the observations, the intensity of the MCD bands for proteins with a sulphur anion of cysteine as proximal haemligand (cytochrome P450 and chloroperoxidase) is predicted to be diminished by at least one order of magnitude compared to that for proteins with an imidazole of a histidine as a protein-derived haemligand (i.e. myoglobin, haemoglobin and horseradish peroxidase).

Item Type: Article
Uncontrolled Keywords: haem electronic structure,haemoproteins,magnetic circular dichroism,near-infrared band assignment,physical and theoretical chemistry ,/dk/atira/pure/subjectarea/asjc/1600/1606
Faculty \ School: Faculty of Science > School of Chemistry
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 19 Jul 2022 17:30
Last Modified: 20 Jul 2022 00:25
URI: https://ueaeprints.uea.ac.uk/id/eprint/86651
DOI: 10.1007/s002140050229

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