Unknown

Dataset Information

0

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


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.

SUBMITTER: Carpena X 

PROVIDER: S-EPMC1369206 | biostudies-other | 2005 Dec

REPOSITORIES: biostudies-other

altmetric image

Publications

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

Carpena Xavier X   Wiseman Ben B   Deemagarn Taweewat T   Singh Rahul R   Switala Jacek J   Ivancich Anabella A   Fita Ignacio I   Loewen Peter C PC  

EMBO reports 20051201 12


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 rea  ...[more]

Similar Datasets

| S-EPMC3183396 | biostudies-literature
| S-EPMC3668122 | biostudies-literature
| S-EPMC4232752 | biostudies-literature
| S-EPMC3513708 | biostudies-literature
| S-EPMC7665192 | biostudies-literature
| S-EPMC2924108 | biostudies-other
| S-EPMC107585 | biostudies-literature
| S-EPMC111410 | biostudies-literature
| S-EPMC3442556 | biostudies-literature
| S-EPMC6377490 | biostudies-literature