Crystal Structure of NADH-cytochrome <I>b<SUB>5</SUB></I>Reductase and Electron Transfer in Flavin-dependent Reductases
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- NISHIDA Hirokazu
- Advanced Research Laboratory, Hitachi, Ltd.
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- MIKI Kunio
- Department of Chemistry, Graduate School of Science, Kyoto University
Bibliographic Information
- Other Title
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- 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
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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
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 38 (1), 73-79, 1996
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679065313408
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- NII Article ID
- 10002024822
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 3934774
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed