A designed functional metalloenzyme that reduces O 2 to H 2O with over one thousand turnovers

Kyle D. Miner, Arnab Mukherjee, Yi Gui Gao, Eric L. Null, Igor D. Petrik, Xuan Zhao, Natasha Yeung, Howard Robinson, Yi Lu

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)5589-5592
Number of pages4
JournalAngewandte Chemie - International Edition
Volume51
Issue number23
DOIs
StatePublished - Jun 4 2012

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Keywords

  • heme proteins
  • metalloproteins
  • oxidoreductases
  • protein design

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Miner, K. D., Mukherjee, A., Gao, Y. G., Null, E. L., Petrik, I. D., Zhao, X., Yeung, N., Robinson, H., & Lu, Y. (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