A designed functional metalloenzyme that reduces O 2 to H 2O with over one thousand turnovers
Abstract
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 O 2 to H 2O 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. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication Title
Angewandte Chemie - International Edition
Recommended Citation
Miner, K., Mukherjee, A., Gao, Y., Null, E., Petrik, I., Zhao, X., Yeung, N., & Robinson, H. (2012). A designed functional metalloenzyme that reduces O 2 to H 2O with over one thousand turnovers. Angewandte Chemie - International Edition, 51 (23), 5589-5592. https://doi.org/10.1002/anie.201201981
