<i>Methylococcus</i> <i>capsulatus</i> cytochrome c’-β (McCP-β) is a heme protein that binds the diatomic gases, NO and CO. The x-ray crystal structure of McCP-β reveals a hydrophobic distal heme pocket containing two phenylalanine residues, Phe 32 and Phe 61, known as the distal Phe cap. Amino acid sequence alignments suggest that the Phe cap is conserved within all known cytochromes c’-β. Here we investigated the influence of Phe cap on the kinetics of NO and CO release, by comparing the reactivity of wild type protein with that of the F61V and F32V variants.

Heme coordination chemistry of cytochrome c' -β: Influence of the distal Phe cap

ACS Spring 2022

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