中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
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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