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EMBO Press, EMBO Reports, 12(6), p. 1156-1162, 2005

DOI: 10.1038/sj.embor.7400550

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A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases

Journal article published in 2005 by Xavier Carpena, Ben Wiseman ORCID, Taweewat Deemagarn, Rahul Singh, Jacek Switala, Anabella Ivancich, Ignacio Fita, Peter C. Loewen
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp.