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A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers


  • We would like to thank Profs. Chad Rienstra and Robert Gennis for the kind use of their oxygen electrodes, Dr. Deborah Stoner-Ma of Brookhaven National Lab (BNL) for help with X-ray data collection of F33Y CuBMb, Dr. Ying-Wu Lin for helpful discussions, and Dr. Nicholas Marshall for help editing this manuscript. This work was supported by the US National Institute of Health (GM062211).


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No spare Tyr: Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O2 to H2O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.

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