ICCAS OpenIR
Molecular mechanism for proton translocation of bacteriorhodopsin
Wang, LP; Li, BF; Jiang, L
2001-06-01
Source PublicationPROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
ISSN1000-3282
Volume28Issue:3Pages:279-282
AbstractBacteriorhodopsin (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.
KeywordBacteriorhodopsin Proton Translocation Retinal Isomerization m Intermediate
Indexed BySCI
Language英语
WOS IDWOS:000169596600001
PublisherSCIENCE PRESS
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Document Type期刊论文
Identifierhttp://ir.iccas.ac.cn/handle/121111/77490
Collection中国科学院化学研究所
AffiliationChinese Acad Sci, Inst Chem, Ctr Mol Sci, Beijing 100080, Peoples R China
Recommended Citation
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.
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