Construction of Artificial Biocatalysts containing a Nonnatural Dinuclear Active Site

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Artificial metalloenzymes containing unnatural multinuclear core were constructed in this project. Dioxygen-binding diiron protein, DcrH-Hr, was studied to elucidate the characteristics and the approaches using a mutation of amino acid residues around the active site led to conversion of the oxygen-binding function. Successful incorporation of a diiron hexacarbonyl core into the protein matrix of cytochrome c provided us artificial hydrogenase capable of photocatalytic hydrogen evolution in an aqueous solution.