A designed functional metalloenzyme that reduces O2 to H2O with over one thousand turnovers

Angew Chem Int Ed Engl. 2012 Jun 4;51(23):5589-92. doi: 10.1002/anie.201201981. Epub 2012 Apr 26.

Abstract

Rational design of functional enzymes with high turnovers is a significant challenge, especially those with complex active site and difficult reactions, such as in respiratory oxidases. Introducing 2 His and 1 Tyr into myoglobin resulted in designed enzymes that reduce O2 to H2O with > 1000 turnovers and minimal release of reactive oxygen species. This also showed that presence and positioning of Tyr, not Cu, are critical for activity.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Biocatalysis
  • Myoglobin / genetics
  • Myoglobin / metabolism*
  • Oxidation-Reduction
  • Oxygen / chemistry*
  • Protein Engineering
  • Protein Structure, Tertiary
  • Reactive Oxygen Species / metabolism
  • Tyrosine / chemistry
  • Tyrosine / metabolism
  • Water / chemistry*

Substances

  • Myoglobin
  • Reactive Oxygen Species
  • Water
  • Tyrosine
  • Oxygen