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- Title
Crystal structure of human heme oxygenase-1.
- Authors
Schuller, D J; Wilks, A; Ortiz de Montellano, P R; Poulos, T L
- 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.
- Publication
Nature structural biology, 1999, Vol 6, Issue 9, p860
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/12319