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A molecular switch and electronic circuit modulate catalase activity in catalase‐peroxidases
Author(s) -
Carpena Xavier,
Wiseman Ben,
Deemagarn Taweewat,
Singh Rahul,
Switala Jacek,
Ivancich Anabella,
Fita Ignacio,
Loewen Peter C
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400550
Subject(s) - catalase , peroxidase , enzyme , chemistry , microbiology and biotechnology , biology , biochemistry
The catalase reaction of catalase‐peroxidases involves catalase‐specific features built into a peroxidase core. An arginine, 20 Å 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 π electron interaction of the heme with the adduct Trp.