Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.

ABSTRACT: Chlorite dismutase-like proteins are structurally closely related to functional chlorite dismutases which are heme b-dependent oxidoreductases capable of reducing chlorite to chloride with simultaneous production of dioxygen. Chlorite dismutase-like proteins are incapable of performing this reaction and their biological role is still under discussion. Recently, members of this large protein family were shown to be involved in heme biosynthesis in Gram-positive bacteria, and thus the protein was renamed HemQ in these organisms. In the present work the structural and heme binding properties of the chlorite dismutase-like protein from the Gram-positive pathogen Listeria monocytogenes (LmCld) were analyzed in order to evaluate its potential role as a regulatory heme sensing protein. The homope

SUBMITTER: Hofbauer S 

PROVIDER: S-EPMC4420033 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature