Cytochrome P450 1A1 opens up to new substrates

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The cytochromes P450 (CYPs) oxidatively transform a huge number of substrates in both prokaryotic and eukaryotic organisms, but the mechanisms by which they accommodate these diverse molecules remain unclear. A new study by Bart and Scott reports two co-crystal structures of CYP1A1 that reveal structural rearrangements and flexible interaction networks that explain how the active site cavity shapes itself around new ligands. These data open the door to an increased understanding of fundamental enzyme behavior and improved searches for anti-cancer compounds.
Original languageEnglish
Article numberjbc.H118.006715
Pages (from-to)19211-19212
Number of pages2
JournalJournal of Biological Chemistry
Issue number50
Publication statusPublished - 14 Dec 2018


  • Cytochrome P450
  • cytochrome P450 1A1
  • crystal structure
  • structural rearrangement

Research Beacons, Institutes and Platforms

  • Biotechnology
  • Energy


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