Display Settings:

Format

Send to:

Choose Destination
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.

Abstract

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

  • Deconstructing heme. [Nat Struct Biol. 1999]
PMID:
10467099
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

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