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Ascorbate peroxidase activity of cytochrome c

Bischin, C and Deac, F and Silaghi-Dumitrescu, R and Worrall, JAR and Rajagopal, BS and Damian, G and Cooper, CE (2011) 'Ascorbate peroxidase activity of cytochrome c.' Free Radical Research, 45 (4). 439 - 444. ISSN 1071-5762

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Abstract

The peroxidase-type reactivity of cytochrome c is proposed to play a role in free radical production and/or apoptosis. This study describes cytochrome c catalysis of peroxide consumption by ascorbate. Under conditions where the sixth coordination position at the cytochrome c heme iron becomes more accessible for exogenous ligands (by carboxymethylation, cardiolipin addition or by partial denaturation with guanidinium hydrochloride) this peroxidase activity is enhanced. A reaction intermediate is detected by stopped-flow UV-vis spectroscopy upon reaction of guanidine-treated cytochrome c with peroxide, which resembles the spectrum of globin Compound II species and is thus proposed to be a ferryl species. The ability of physiological levels of ascorbate (10μM) to interact with this species may have implications for mechanisms of cell signalling or damage that are based on cytochrome c/peroxide interactions. © 2011 Informa UK, Ltd.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 23 Sep 2011 08:53
Last Modified: 14 Oct 2019 17:19
URI: http://repository.essex.ac.uk/id/eprint/796

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