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Redox equilibration after one-electron reduction of cytochrome c oxidase: Radical formation and a possible hydrogen relay mechanism

Ashe, D and Alleyne, T and Wilson, M and Svistunenko, D and Nicholls, P (2014) 'Redox equilibration after one-electron reduction of cytochrome c oxidase: Radical formation and a possible hydrogen relay mechanism.' Archives of Biochemistry and Biophysics, 554. 36 - 43. ISSN 0003-9861

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Abstract

Kinetic studies using UV/visible and EPR spectroscopy were carried out to follow the distribution of electrons within beef heart cytochrome c oxidase (CcO), both active and cyanide-inhibited, following addition of reduced cytochrome c as electron donor. In the initial one-electron reduced state the electron is shared between three redox centers, heme a, CuA and a third site, probably CuB. Using a rapid freeze system and the spin trap 5,5-dimethyl-1- pyrroline N-oxide (DMPO) a protein radical was also detected. The EPR spectrum of the DMPO adduct of this radical was consistent with tyrosyl radical capture. This may be a feature of a charge relay mechanism involved in some part of the CcO electron transfer system from bound cytochrome c via CuA and heme a to the a3CuB binuclear center. © 2014 Elsevier Inc. All rights reserved.

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: 03 Jul 2015 06:31
Last Modified: 19 Jun 2019 10:15
URI: http://repository.essex.ac.uk/id/eprint/14174

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