Send to:

Choose Destination
See comment in PubMed Commons below
Nat Struct Biol. 1999 Sep;6(9):860-7.

Crystal structure of human heme oxygenase-1.

Author information

  • 1Departments of Molecular Biology and Biochemistry, and Physiology and Biophysics, and Program in Macromolecular Structure, University of California, Irvine, California 92697-3900, USA.


Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme iron ligand, His 25. Conserved glycines in the distal helix near the oxygen binding site allow close contact between the helix backbone and heme in addition to providing flexibility for substrate binding and product release. Regioselective oxygenation of the alpha-meso heme carbon is due primarily to steric influence of the distal helix.

Comment in

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Write to the Help Desk