A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.
Publication Type:Journal Article
Source:J Am Chem Soc, Volume 142, Issue 28, p.11978-11982 (2020)
<p>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)═O 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)═O porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O or HO. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology.</p>