Issue 13, 2011
From the journal:

Organic & Biomolecular Chemistry

Peroxidase activity enhancement of horse cytochrome c by dimerization†

Zhonghua Wang,ab   Takashi Matsuo,a   Satoshi Nagaoa  and  Shun Hirota*a  

* Corresponding authors

a Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Japan
E-mail: hirota@ms.naist.jp
Fax: (+81)-743-72-6119
Tel: (+81)-743-72-6110

b College of Chemistry and Chemical Engineering, China West Normal University, Nanchong, China

Abstract

The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin π-cation radical) species were detected in the reactions with hydrogen peroxide and meta-chloroperbenzoic acid, respectively. These results show that oligomeric cytochrome c can contribute as a proapoptotic conformer by the increased peroxidase activity.

Graphical abstract: Peroxidase activity enhancement of horse cytochrome c by dimerization

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Article information

DOI
https://doi.org/10.1039/C1OB05552F
Article type
Communication
Submitted
07 Apr 2011
Accepted
12 Apr 2011
First published
12 Apr 2011

Org. Biomol. Chem., 2011,9, 4766-4769

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Peroxidase activity enhancement of horse cytochrome c by dimerization

Z. Wang, T. Matsuo, S. Nagao and S. Hirota, Org. Biomol. Chem., 2011, 9, 4766 DOI: 10.1039/C1OB05552F

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