Structural Study of Ferredoxin-Dependent Bilin Reductase

• SUGISHIMA Masakazu

  Kurume University School of Medicine, JSPS research fellow

• HAGIWARA Yoshinori

  Department of Biological Science, Graduate School of Science, Osaka University

• TAKAHASHI Yasuhiro

  Department of Biological Science, Graduate School of Science, Osaka University

• FUKUYAMA Keiichi

  Department of Biological Science, Graduate School of Science, Osaka University

Bibliographic Information

Other Title

• フェレドキシン依存性ビリン還元酵素の構造研究
• サイキン ノ ケンキュウ カラ フェレドキシン イゾンセイ ビリン カンゲン コウソ ノ コウゾウ ケンキュウ

Abstract

Phytobilins, linear tetrapyrrole pigments utilized for light-harvesting and light-sensing in photosynthetic organisms, are synthesized from biliverdin by ferredoxin-dependent bilin reductases (FDBRs) . We have determined the crystal structures of substrate-free and substrate-bound forms of PcyA, one such FDBR. These structures revealed the first tertiary structures of an FDBR family member. Based on these structures, we discuss the binding mechanisms of ferredoxin and substrate to PcyA. Moreover, we propose the reaction mechanism how PcyA controls the two-step reductions of biliverdin. Homology modeling of other FDBRs using PcyA structure may provide structural bases for the reaction mechanisms of other FDBRs.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 48 (4), 283-289, 2006

  The Crystallographic Society of Japan

Details

• CRID: 1390001204086548992
• NII Article ID: 10019293665
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.48.283
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 8084498
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8084498
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed