Volume 145, 2010
From the journal:

Faraday Discussions

Radicals in enzymatic catalysis—a thermodynamic perspective

Johnny Hioea  and  Hendrik Zipse*a  

* Corresponding authors

a Department of Chemistry and Biochemistry, LMU München, Butenandtstrasse 5–13, München, Germany
E-mail: zipse@cup.uni-muenchen.de

Abstract

The thermodynamic stability of radicals involved in enzymatic catalysis has been quantified using a series of theoretical methods. It is found that three of the most often encountered radicals located on the enzyme protein chain (tyrosyl, cysteinyl and glycyl radicals) are of similar stability. This is despite the fact that O–H, S–H and C–H bonds have intrinsically very different homolytic bond dissociation energies. The cofactor-derived 5′-adenosyl radical, in contrast, is significantly less stable than these protein-bound radicals.

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Article information

DOI
https://doi.org/10.1039/B907121K
Article type
Paper
Submitted
07 Apr 2009
Accepted
21 May 2009
First published
22 Sep 2009

Faraday Discuss., 2010,145, 301-313

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Radicals in enzymatic catalysis—a thermodynamic perspective

J. Hioe and H. Zipse, Faraday Discuss., 2010, 145, 301 DOI: 10.1039/B907121K

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