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One aim in our laboratory is to use small,soluble protein scaffold,and the genetic incorporation of unnatural amino acid to design easy-to-characterize,easy-to-produce,and easy-to-optimize metalloenzymes which catalyze these important reactions with equal or greater efficiency/selectivity than that of the natural systems.Through the genetic incorporation of the Tyr-His ligand and CuB site into myoglobin,we recapitulated important features of HCO into this small soluble protein,which exhibits selective O2 reduction activity while generating less than 6%ROS,at more than 1000 turnovers.These results support that Tyr-His crosslink is indeed important for HCO function,and creates the exciting opportunity to rapidly evolve better HCO model proteins to achieve higher activity and selectivity,which may be suitable as alternatives to precious metal catalyst in fuel cells.Another aspect of our ongoing research is the development of new methods for precise attachment of functional metal complexes on biomolecules,which is an important strategy for metalloprotein design.Bioorthogonal chemical reactions together with genetic code expansion technique have provided exciting new means for protein labeling in living cells.The main advantages of photoclick reaction are its fast rate(up to 50M-1S-1),and that it has no need for toxic copper catalyst.