Structural and redox properties of the leaderless DsbE (CcmG) protein: Both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm
文献类型：期刊论文
| 作者 | Li, Q; Hu, HY; Wang, WQ; Xu, GJ |
| 刊名 | BIOLOGICAL CHEMISTRY
 |
| 出版日期 | 2001 |
| 卷号 | 382期号:12页码:1679-1686 |
| 关键词 | active-site cysteine DsbE protein redox reduced structure thiol-disulfide |
| 通讯作者 | Li, Q (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China., |
| 英文摘要 | The thiol/disulfide oxidoreductases play important roles in ensuring the correct formation of disulfide bonds, of which the DsbE protein, also called CcmG, is the one implicated in electron transfer for cytochrome c maturation in the periplasm of Escherichia coli. The soluble, N-terminally truncated DsbE was overexpressed and purified to homogeneity. Here we report the structural and redox properties of the leaderless form (DsbEL(-)). During the redox reaction, the protein undergoes a structural transformation resulting in a more stable reduced form, but this form shows very low reactivity in thiol/disulfide exchange of cysteine residues and low activity in accelerating the reduction of insulin. The standard redox potential (E'(0)) for the active thiol/disulfide was determined to be -0.186 V, only one of the two cysteines (Cys80) was suggested to be the active residue in the redox reaction. From the aspect of biochemical properties, DsbE can be regarded as a weak reductant in the Escherichia coli periplasm. This implies that the function of DsbE in cytochrome c maturation can be ascribed to its active-site cysteines and the structure of the reduced form. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | DISULFIDE BOND FORMATION ; THIOREDOXIN-LIKE PROTEIN ; CYTOCHROME-C ; EFFICIENT CATALYSIS ; ELECTRON-TRANSFER ; FORMATION INVIVO ; ISOMERASE DSBA ; IN-VIVO ; OXIDOREDUCTASES ; BIOGENESIS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000173656100006 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2707]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Li, Q,Hu, HY,Wang, WQ,et al. Structural and redox properties of the leaderless DsbE (CcmG) protein: Both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm[J]. BIOLOGICAL CHEMISTRY,2001,382(12):1679-1686. |
| APA | Li, Q,Hu, HY,Wang, WQ,&Xu, GJ.(2001).Structural and redox properties of the leaderless DsbE (CcmG) protein: Both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm.BIOLOGICAL CHEMISTRY,382(12),1679-1686. |
| MLA | Li, Q,et al."Structural and redox properties of the leaderless DsbE (CcmG) protein: Both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm".BIOLOGICAL CHEMISTRY 382.12(2001):1679-1686. |
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