A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases |
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Authors: | Carpena Xavier Wiseman Ben Deemagarn Taweewat Singh Rahul Switala Jacek Ivancich Anabella Fita Ignacio Loewen Peter C |
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Institution: | Department of Microbiology, University of Manitoba, Winnipeg MB R3T 2N2, Canada. |
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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. |
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