Crystal structure of rat heme oxygenase-1 in complex with heme

Masakazu Sugishima, Yoshiaki Omata, Yoshimitsu Kakuta, Hiroshi Sakamoto, Masato Noguchi, Keiichi Fukuyama

研究成果: ジャーナルへの寄稿学術誌査読

138 被引用数 (Scopus)

抄録

Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O2 and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the δ-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH-. The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed. Copyright (C) 2000 Federation of European Biochemical Societies.

本文言語英語
ページ(範囲)61-66
ページ数6
ジャーナルFEBS Letters
471
1
DOI
出版ステータス出版済み - 4月 7 2000
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

フィンガープリント

「Crystal structure of rat heme oxygenase-1 in complex with heme」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル