Volume 148, 2011
From the journal:

Faraday Discussions

Dissecting the mechanism of oxygen trafficking in a metalloenzyme†

Mark A. Smith,‡a   Peter F. Knowles,a   Michael J. McPhersona  and  Arwen R. Pearson*a  

* Corresponding authors

a Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK
E-mail: a.r.pearson@leeds.ac.uk
Fax: +44 113 3435638
Tel: +44 113 3433032

Abstract

A key question in the biological activation of oxygen is how the protein matrix regulates the delivery of oxygen to its site of activation. We are using Escherichia colicopper amine oxidase as a model system to investigate the roles played by both local active site residues as well as long range interactions in this process. We have generated active site mutants, as well as mutants in the putative oxygen delivery channel and characterised their affects on enzyme structure and catalysis.

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Article information

DOI
https://doi.org/10.1039/C005054G
Article type
Paper
Submitted
13 Apr 2010
Accepted
28 Apr 2010
First published
23 Sep 2010

Faraday Discuss., 2011,148, 269-282

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Dissecting the mechanism of oxygen trafficking in a metalloenzyme

M. A. Smith, P. F. Knowles, M. J. McPherson and A. R. Pearson, Faraday Discuss., 2011, 148, 269 DOI: 10.1039/C005054G

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