Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant
文献类型:期刊论文
作者 | Li, Q; Hu, HY; Xu, GJ |
刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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出版日期 | 2001 |
卷号 | 283期号:4页码:849-853 |
关键词 | DsbE protein thioredoxin domain biochemical characterization thiol/disulfide redox reaction reductant |
通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, 320 Yueyang Rd, Shanghai 200031, Peoples R China., |
英文摘要 | Thioredoxin (Trx) domain is a typical fold functioning in thiol/disulfide exchange. DsbE protein is one of the Trx-domain containing proteins involved in electron transfer for cytochrome c maturation in the periplasm of Escherichia coli. The soluble C-terminal Trx domain of DsbE protein was overexpressed and purified to homogeneity. We herein report biochemical characterization of the structural and redox properties of this domain. During redox reaction, the domain undergoes a structural transformation resulting in a more stable reduced form with a free energy difference (Delta DeltaG(Redox)) of ca. 5 kcal/mol, but the thiol/disulfide exchange exhibits very low reactivity. The standard redox potential (E-0') for the active thiol/disulfide is -0.175 V and the pK(a) value of the active cysteine is around 6.8, indicating that the domain acts as a weak reductant. This implies that the membrane-anchored DsbE protein may provide driven reducing power for the redox reaction in the thiol/disulfide exchange pathway. (C) 2001 Academic Press. |
学科主题 | Biochemistry & Molecular Biology; Biophysics |
类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
关键词[WOS] | DISULFIDE-ISOMERASE DSBA ; REDOX PROPERTIES ; BACTERIAL PERIPLASM ; CRYSTAL-STRUCTURE ; BOND FORMATION ; IN-VIVO ; PATHWAYS ; PH |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000168928400021 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/2651] ![]() |
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,Xu, GJ. Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2001,283(4):849-853. |
APA | Li, Q,Hu, HY,&Xu, GJ.(2001).Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,283(4),849-853. |
MLA | Li, Q,et al."Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 283.4(2001):849-853. |
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