Molecular mechanism for proton translocation of bacteriorhodopsin
文献类型:期刊论文
作者 | Wang, LP; Li, BF; Jiang, L |
刊名 | PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
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出版日期 | 2001-06-01 |
卷号 | 28期号:3页码:279-282 |
关键词 | Bacteriorhodopsin Proton Translocation Retinal Isomerization m Intermediate |
ISSN号 | 1000-3282 |
英文摘要 | Bacteriorhodopsin (bR) is the sole protein in the purple membrane of Halobacterium salinarium, which functions as proton pump, charge separation and photochromism. The chromophore retinal is covalently attached to Lys 216 via a protonated Schiff base. Upon illumination, the all-trans to 13-cis isomerization of the retinal results in deprotonation of the Schiff base followed by alterations in protonatable groups within bacteriorhodopsin. The changed force field induces changes, even in the tertiary structure, which facilitate and warrant the vectorial proton translocation. |
语种 | 英语 |
WOS记录号 | WOS:000169596600001 |
出版者 | SCIENCE PRESS |
源URL | [http://ir.iccas.ac.cn/handle/121111/77489] ![]() |
专题 | 中国科学院化学研究所 |
作者单位 | Chinese Acad Sci, Inst Chem, Ctr Mol Sci, Beijing 100080, Peoples R China |
推荐引用方式 GB/T 7714 | Wang, LP,Li, BF,Jiang, L. Molecular mechanism for proton translocation of bacteriorhodopsin[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2001,28(3):279-282. |
APA | Wang, LP,Li, BF,&Jiang, L.(2001).Molecular mechanism for proton translocation of bacteriorhodopsin.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,28(3),279-282. |
MLA | Wang, LP,et al."Molecular mechanism for proton translocation of bacteriorhodopsin".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 28.3(2001):279-282. |
入库方式: OAI收割
来源:化学研究所
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