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EMBO Rep. 2005 Dec;6(12):1156-62.

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

Author information

1
Department of Microbiology, University of Manitoba, Winnipeg MB R3T 2N2, Canada.

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.

PMID:
16211084
PMCID:
PMC1369206
DOI:
10.1038/sj.embor.7400550
[Indexed for MEDLINE]
Free PMC Article

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