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Volume 145, 2010
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Radicals in enzymatic catalysis—a thermodynamic perspective

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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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The article was received on 07 Apr 2009, accepted on 21 May 2009 and first published on 22 Sep 2009

Article type: Paper
DOI: 10.1039/B907121K
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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