| Autor: |
Carpena, Xavier, Wiseman, Ben, Deemagarn, Taweewat, Singh, Rahul, Switala, Jacek, Ivancich, Anabella, Fita, Ignacio, Loewen, Peter C. |
| Předmět: |
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| Zdroj: |
EMBO Reports; Dec2005, Vol. 6 Issue 12, p1156-1162, 7p, 5 Diagrams, 2 Charts |
| Abstrakt: |
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 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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