How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.

ABSTRACT: The most striking feature of mammalian peroxidases, including myeloperoxidase and lactoperoxidase (LPO) is the existence of covalent bonds between the prosthetic group and the protein, which has a strong impact on their (electronic) structure and biophysical and chemical properties. Recently, a novel bacterial heme peroxidase with high structural and functional similarities to LPO was described. Being released from Escherichia coli, it contains mainly heme b, which can be autocatalytically modified and covalently bound to the protein by incubation with hydrogen peroxide. In the present study, we investigated the reactivity of these two forms in their ferric, compound I and compound II state in a multi-mixing stopped-flow study. Upon heme modification, the reactions between the ferric prote

SUBMITTER: Auer M 

PROVIDER: S-EPMC4223346 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature