Issue 11, 2012
From the journal:

Catalysis Science & Technology

The Met80Ala point mutation enhances the peroxidase activity of immobilized cytochromec†

Antonio Ranieri,a   Fabrizio Bernini,a   Carlo Augusto Bortolottia  and  Elena Castellini*a  

* Corresponding authors

a Department of Chemistry, University of Modena and Reggio Emilia, Via Campi 183, I-41125 Modena, Italy
E-mail: elena.castellini@unimore.it
Fax: +39 059373543
Tel: +39 0592055113

Abstract

The effects of replacement of the axial methionine 80 heme ligand with a non-coordinating alanine on the peroxidase activity of kaolinite-immobilized cytochrome c were investigated at different pH values. The catalytic activity of the adsorbed mutant was found to be remarkably higher than that of wild-type cytochrome c. The pH dependence of Vmax and KM values is discussed in terms of accessibility of the substrates to the metal center and surface charge of kaolinite. Our approach, based on the combined use of adsorption on kaolinite and protein engineering, endows this bioinorganic interface with remarkable catalytic properties.

Graphical abstract: The Met80Ala point mutation enhances the peroxidase activity of immobilized cytochrome c

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Article information

DOI
https://doi.org/10.1039/C2CY20347B
Article type
Communication
Submitted
21 Nov 2011
Accepted
08 Jul 2012
First published
09 Jul 2012

Catal. Sci. Technol., 2012,2, 2206-2210

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The Met80Ala point mutation enhances the peroxidase activity of immobilized cytochrome c

A. Ranieri, F. Bernini, C. A. Bortolotti and E. Castellini, Catal. Sci. Technol., 2012, 2, 2206 DOI: 10.1039/C2CY20347B

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