Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b.

ABSTRACT: The H₂O₂-dependent oxidative decarboxylation of coproheme III is the final step in the biosynthesis of heme b in many microbes. However, the coproheme decarboxylase reaction mechanism is unclear. The structure of the decarboxylase in complex with coproheme III suggested that the substrate iron, reactive propionates, and an active-site tyrosine convey a net 2e^-/2H⁺ from each propionate to an activated form of H₂O₂ Time-resolved EPR spectroscopy revealed that Tyr-145 formed a radical species within 30 s of the reaction of the enzyme-coproheme complex with H₂O₂ This radical disappeared over the next 270 s, consistent with a catalytic intermediate. Use of the harderoheme III intermediate as substrate

SUBMITTER: Streit BR 

PROVIDER: S-EPMC5857992 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature