2014年2月
Structural insights into the function of a thermostable copper-containing nitrite reductase
JOURNAL OF BIOCHEMISTRY
ダウンロード
回数 : 79
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- 巻
- 155
- 号
- 2
- 開始ページ
- 123
- 終了ページ
- 135
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1093/jb/mvt107
- 出版者・発行元
- OXFORD UNIV PRESS
Copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO(-)2)to nitric oxide (NO) during denitrification. We determined the crystal structures of CuNIR from thermophilic gram-positive bacterium, Geobacillus thermodenitrificans (GtNIR) in chloride- and formate-bound forms of wild type at 1.15 A resolution and the nitrite-bound form of the C135A mutant at 1.90 A resolution. The structure of C135A with nitrite displays a unique eta(1)-O coordination mode of nitrite at the catalytic copper site (T2Cu), which has never been observed at the T2Cu site in known wild-type CuNIRs, because the mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. A detailed comparison of the WT structure with the nitrite-bound C135A structure implies the replacement of hydrogen-bond networks around His244 and predicts the flow path of protons consumed by nitrite reduction. On the basis of these observations, the reaction mechanism of GtNIR through the eta(1)-O coordination manner is proposed.
- リンク情報
- ID情報
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- DOI : 10.1093/jb/mvt107
- ISSN : 0021-924X
- eISSN : 1756-2651
- PubMed ID : 24293549
- Web of Science ID : WOS:000330895000007