Electronic State of the His/Tyr-Ligated Heme of BthA by Mossbauer and DFT Analysis.

ABSTRACT: The BthA protein from the microorganism Burkholderia thailandensis contains two hemes with axial His/OH₂ and His/Tyr coordinations separated by the closest interheme distance of 14 Å. BthA has a similar structure and belongs to the same family of multiheme cytochrome c peroxidases as MauG, which performs long-range oxidation of the partner protein methylamine dehydrogenase. Magnetic Mössbauer spectroscopy of the diferric state of BthA corroborates previous structural work identifying a high-spin (His/OH₂) peroxidatic heme and a low-spin (His/Tyr) electron transfer heme. Unlike MauG, addition of H₂O₂ fully converts the diferric form of BthA to a stable 2e^- oxidized state, allowing a new assessment of this state. The peroxi

SUBMITTER: Weitz AC 

PROVIDER: S-EPMC8049104 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature