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

AuthorsCarpena, Xavi ; Wiseman, Ben; Deemagarn, Taweewat; Singh, Rahul; Switala, Jacek; Ivancich, Anabella; Fita, Ignacio ; Loewen, Peter C.
Issue Date7-Oct-2005
PublisherNature Publishing Group
CitationEMBO Reports 6(12): 1156-1162 (2005)
AbstractThe 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 H2O2, 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. © 2005 European Molecular Biology Organization.
Publisher version (URL)http://dx.doi.org/10.1038/sj.embor.7400550
Identifiersdoi: 10.1038/sj.embor.7400550
issn: 1469-221X
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