Article
A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.
Journal of the American Chemical Society - 15 Jul 2020
Rizzolo Kimberly, Weitz Andrew C, Cohen Steven E, Drennan Catherine L, Hendrich Michael P, Elliott Sean J
Abstract excerpt
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...
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