Spectroscopic evidence of the effect of hydrogen peroxide excess on the coproheme decarboxylase from actinobacterial <i>Corynebacterium diphtheriae</i>.

ABSTRACT: The actinobacterial coproheme decarboxylase from Corynebacterium diphtheriae catalyzes the final reaction to generate heme b via the "coproporphyrin-dependent" heme biosynthesis pathway in the presence of hydrogen peroxide. The enzyme has a high reactivity toward H₂O₂ used for the catalytic reaction and in the presence of an excess of H₂O₂ new species are generated. Resonance Raman data, together with electronic absorption spectroscopy and mass spectrometry, indicate that an excess of hydrogen peroxide for both the substrate (coproheme) and product (heme b) complexes of this enzyme causes a porphyrin hydroxylation of ring C or D, which is compatible with the formation of an iron chlorin-type heme d species. A similar e

SUBMITTER: Sebastiani F 

PROVIDER: S-EPMC9310987 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature