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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2011/07 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue |
| 執筆形態 | その他 |
| 掲載誌名 | FEBS JOURNAL |
| 出版社・発行元 | WILEY-BLACKWELL |
| 巻・号・頁 | 278(13),pp.2387-2394 |
| 著者・共著者 | Toru Yoshida,Hideaki Tsuge,Hiroki Konno,Toru Hisabori,Yasushi Sugano |
| 概要 | The dye-decolorizing peroxidase (DyP)-type peroxidase family is a unique heme peroxidase family. The primary and tertiary structures of this family are obviously different from those of other heme peroxidases. However, the details of the structure function relationships of this family remain poorly understood. We show four high-resolution structures of DyP (EC 1.11.1.19), which is representative. of this family: the native DyP (1.40 angstrom), the D171N mutant DyP (1.42 angstrom), the native DyP complexed with cyanide (1.45 angstrom), and the D171N mutant DyP associated with cyanide (1.40 angstrom). These structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. Moreover, these structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron. On the basis of these results, we propose a swing mechanism ill compound I formation. When DyP reacts with hydrogen peroxide, OD2 swings towards an optimal position to accept the proton from hydrogen peroxide bound to the heme iron. |
| DOI | 10.1111/j.1742-4658.2011.08161.x |
| ISSN | 1742-464X |