Reactivity of Myoglobin Reconstituted with Cobalt Corrole toward Hydrogen Peroxide

The protein matrix of natural metalloenzymes regulates the reactivity of metal complexes to establish unique catalysts. We describe the incorporation of a cobalt complex of corrole (CoCor), a trianionic porphyrinoid metal ligand, into an apo-form of myoglobin to provide a reconstituted protein (rMb(CoCor)). This protein was characterized by UV-vis, EPR, and mass spectroscopic measurements. The reaction of rMb(CoCor) with hydrogen peroxide promotes an irreversible oxidation of the CoCor cofactor, whereas the same reaction in the presence of a phenol derivative yields the cation radical form of CoCor. Detailed kinetic investigations indicate the formation of a transient hydroperoxo complex of rMb(CoCor) which promotes the oxidation of the phenol derivatives. This mechanism is significantly different for native heme-dependent peroxidases, which generate a metal-oxo species as an active intermediate in a reaction with hydrogen peroxide. The present findings of unique reactivity will contribute to further design of artificial metalloenzymes.

Automated summary

The incorporation of a cobalt complex of corrole (CoCor) into an apo-form of myoglobin to provide a reconstituted protein (rMb(CoCor)) was characterized by UV-vis, EPR, and mass spectroscopic measurements. Reaction of rMb(CoCor) with hydrogen peroxide leads to irreversible oxidation of the CoCor cofactor, while the same reaction in the presence of a phenol derivative yields the cation radical form of CoCor. Detailed kinetic investigations suggest the formation of a transient hydroperoxo complex of rMb(CoCor) which promotes the oxidation of phenol derivatives.