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Keywords:

  • alkane oxidation;
  • heme proteins;
  • iron;
  • metalloenzymes;
  • protein engineering
Thumbnail image of graphical abstract

A NADH turnover rate of 741 min−1 in the oxidition of ethane to ethanol is observed with an engineered form of the heme monooxygenase cytochrome P450cam—the first example of such activity for a P450 enzyme (GC analysis shown). Ethanol is formed at 78 min−1 (10.5 % coupling). The mutant is ≈45 % high-spin in the absence of substrate, making it a useful platform for P450 structure–function studies.