Crystal Structure of NADH-cytochrome <I>b<SUB>5</SUB></I>Reductase and Electron Transfer in Flavin-dependent Reductases

• NISHIDA Hirokazu

  Advanced Research Laboratory, Hitachi, Ltd.

• MIKI Kunio

  Department of Chemistry, Graduate School of Science, Kyoto University

Bibliographic Information

Other Title

• NADH-チトクロム<I>b<SUB>5</SUB></I>還元酵素の結晶構造とフラビン依存性還元酵素での電子伝達
• NADH チトクロム b5 カンゲン コウソ ノ ケッショウ コウゾウ ト フ

Abstract

The structure of NADH-cytochrome bs reductase has been determined and refined at 2.1 Å resolution. The molecular structure reveals its two domain nature, the FAD binding domain and the NADH domain. Structural difference between the FAD-binding site of this enzyme and that of ferredoxin-NADP⁺ reductase gives an explanation about the difference of their enzymatic reaction with nucleotides. Three conserved amino acid residues interact significantly with the flavin molecules in four flavin-dependent reductases whose molecular structures have a similar folding pattern in spite of their relative low sequence identity. The electrostatic potentials on the molecular surfaces were compared among these four flavin-dependent reductases and their electron-transfer partners.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 38 (1), 73-79, 1996

  The Crystallographic Society of Japan

Details

• CRID: 1390282679065313408
• NII Article ID: 10002024822
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.38.73
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 3934774
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3934774
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed