Article
Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b.
The Journal of biological chemistry - 16 Mar 2018
Streit Bennett R, Celis Arianna I, Moraski Garrett C, Shisler Krista A, Shepard Eric M, Rodgers Kenton R, Lukat-Rodgers Gudrun S, DuBois Jennifer L
Abstract excerpt
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...
Topics
- Carboxy-Lyases
- Catalysis
- Catalytic Domain
- Crystallography, X-Ray
- Decarboxylation
- Electron Spin Resonance Spectroscopy
- Ferric Compounds
- Free Radicals
- Heme
- Hydrogen Peroxide
- Kinetics
- Models, Molecular
- Mutation