Structural highlights
Publication Abstract from PubMed
BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV) horizontal lineO oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here, we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV) horizontal lineO porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O2 or H2O2. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology.
A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.,Rizzolo K, Weitz AC, Cohen SE, Drennan CL, Hendrich MP, Elliott SJ J Am Chem Soc. 2020 Jul 1. doi: 10.1021/jacs.0c04023. PMID:32564595[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rizzolo K, Weitz AC, Cohen SE, Drennan CL, Hendrich MP, Elliott SJ. A Stable Ferryl Porphyrin at the Active Site of Y463M BthA. J Am Chem Soc. 2020 Jul 1. doi: 10.1021/jacs.0c04023. PMID:32564595 doi:http://dx.doi.org/10.1021/jacs.0c04023
