The catalytic mechanism of cytochrome P450 BM3 involves a 6 A movement of the bound substrate on reduction

Nat Struct Biol. 1996 May;3(5):414-7. doi: 10.1038/nsb0596-414.
No abstract available

Publication types

  • Comparative Study
  • Letter

MeSH terms

  • Bacillus megaterium / enzymology
  • Bacterial Proteins*
  • Camphor 5-Monooxygenase
  • Computer Simulation
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / metabolism*
  • Hydroxylation
  • Laurates / chemistry
  • Laurates / metabolism*
  • Magnetic Resonance Spectroscopy
  • Mixed Function Oxygenases / chemistry
  • Mixed Function Oxygenases / metabolism*
  • Models, Molecular
  • Movement
  • NADPH-Ferrihemoprotein Reductase
  • Oxidation-Reduction

Substances

  • Bacterial Proteins
  • Laurates
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • Camphor 5-Monooxygenase
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases