Capturing a bis-Fe(IV) State in Methylosinus trichosporium OB3b MbnH.

ABSTRACT: The diheme bacterial cytochrome c peroxidase (bCcP)/MauG superfamily is a diverse set of enzymes that remains largely uncharacterized. One recently discovered member, MbnH, converts a tryptophan residue in its substrate protein, MbnP, to kynurenine. Here we show that upon reaction with H₂O₂, MbnH forms a bis-Fe(IV) intermediate, a state previously detected in just two other enzymes, MauG and BthA. Using absorption, Mössbauer, and electron paramagnetic resonance (EPR) spectroscopies coupled with kinetic analysis, we characterized the bis-Fe(IV) state of MbnH and determined that this intermediate decays back to the diferric state in the absence of MbnP substrate. In the absence of MbnP substrate, MbnH can also detoxify H₂O₂

SUBMITTER: Manesis AC 

PROVIDER: S-EPMC10083075 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature