Heme proteins reconstitutional modification

Figure 42. The preparation of a photoenzyme by the reconstitution of a heme protein with Co(II)-protoporphyrin IX and the chemical modification of the protein backbone with a tethered chro-mophore. Hydrogen evolution and hydrogenation of acetylene derivatives photobiocatalyzed by the assembly.

The initial turnover number of the thioanisole oxidation by the reconstituted Mb is clearly larger than that observed for the native Mb, and the kcat/Km value is more than seven fold higher than that of the native protein. The epoxidation of styrene is also effectively catalyzed by the reconstituted Mb by 10-fold increase compared to native Mb. These findings indicate that the appropriate modification of the heme propionate side chains forms a substrate-binding domain that enhances the peroxidase and peroxygenase activities of Mb, as shown in Table VI. 

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