Coordination of the N-Terminal Heme in the Non-Classical Peroxidase from Escherichia coli.

ABSTRACT: The non-classical bacterial peroxidase from Escherichia coli, YhjA, is proposed to deal with peroxidative stress in the periplasm when the bacterium is exposed to anoxic environments, defending it from hydrogen peroxide and allowing it to thrive under those conditions. This enzyme has a predicted transmembrane helix and is proposed to receive electrons from the quinol pool in an electron transfer pathway involving two hemes (NT and E) to accomplish the reduction of hydrogen peroxide in the periplasm at the third heme (P). Compared with classical bacterial peroxidases, these enzymes have an additional N-terminal domain binding the NT heme. In the absence of a structure of this protein, several residues (M82, M125 and H134) were mutated to identify the axial ligand of the NT heme. Spe

SUBMITTER: Oliveira RNS 

PROVIDER: S-EPMC10301912 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature