Autor:	A Wilks, David J. Schuller, Ortiz de Montellano Pr, Thomas L. Poulos
Rok vydání:	1999
Předmět:	Stereochemistry Ligand Biochemistry Heme oxygenase chemistry.chemical_compound Protein structure chemistry Structural Biology Helix Genetics Protein folding Binding site Heme Oxygen binding
Zdroj:	Nature Structural Biology. 6:860-867
ISSN:	1072-8368
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::124bae03030c0736637f75471f157bd6 https://doi.org/10.1038/12319 Zobrazit plný text záznamu Full text from SpringerLink