Reactivity of canonical bacterial cytochrome <i>c</i> peroxidases: insights into the electronic structure of compound I.

ABSTRACT: Bacterial cytochrome c peroxidase (bCcP) family members include di-heme enzymes that are capable of producing various high oxidation states in their reactions with the substrate H₂O₂. Canonical family members such as the enzyme from Nitrosomonas europaea (Ne) are responsible for the detoxification of H₂O₂ in the periplasm of many Gram negative organisms. Elucidation of the electronic structure of the kinetic intermediates for canonical bCcP enzymes has yet to be attained, though the orthologs MauG and others have evoked a Fe(iv)Fe(iv)[double bond, length as m-dash]O species capable of long-range oxidation. Here, we use a combination of optical, electron paramagnetic and Mössbauer spectroscopies to demonstrate that the species

SUBMITTER: Hewitt P 

PROVIDER: S-EPMC11892367 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature