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Nitrite binding to globins: Linkage isomerism, EPR silence and reductive chemistry

Silaghi-Dumitrescu, R and Svistunenko, DA and Cioloboc, D and Bischin, C and Scurtu, F and Cooper, CE (2014) 'Nitrite binding to globins: Linkage isomerism, EPR silence and reductive chemistry.' Nitric Oxide - Biology and Chemistry, 42. 32 - 39. ISSN 1089-8603

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Abstract

© 2014 The Authors. The nitrite adducts of globins can potentially bind via O- or N- linkage to the heme iron. We have used EPR (electron paramagnetic resonance) and DFT (density functional theory) to explore these binding modes to myoglobin and hemoglobin. We demonstrate that the nitrite adducts of both globins have detectable EPR signals; we provide an explanation for the difficulty in detecting these EPR features, based on uniaxial state considerations. The EPR and DFT data show that both nitrite linkage isomers can be present at the same time and that the two isomers are readily interconvertible in solution. The millisecond-scale process of nitrite reduction by Hb is investigated in search of the elusive Fe(II)-nitrite adduct.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 16 Sep 2014 09:40
Last Modified: 06 Feb 2018 20:15
URI: http://repository.essex.ac.uk/id/eprint/10206

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