X-ray Crystallographic Structure of the Novel Multipleheme Enzyme, Hydroxylamine Oxidoreductase from Nitrosomonas Europaea.
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- IGARASHI Noriyuki
- Institute of Materials Structure Science, High Energy Accelerator Research Organization
Bibliographic Information
- Other Title
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- 新規の多ヘム酵素の立体構造解明
- シンキ ノ タヘム コウソ ノ リッタイ コウゾウ カイメイ ニホン ケッショウ ガッカイ ガッカイショウ ジュショウ ロンブン
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Abstract
The 2.8Å crystal structure of the novel multiple-heme enzyme, hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosonnonas europaea, is described. Twenty-four hemes lie in the center bottom of the trimeric molecule, localized in four clusters within each monomer. The heme clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet occupied by the novel heme, heme P460. The structure suggests pathways by which ‘dielectron transfer’ may occur through the precisely arranged hemes.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 41 (5), 283-292, 1999
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679063323392
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- NII Article ID
- 10013628754
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 4894712
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed