منابع مشابه
Carboxyl groups and the proton pump of bacteriorhodopsin.
The purple membrane isolated from Halobacterium halobium contains only a single protein, bacteriorhodopsin, which functions as a light-driven proton pump. Substantial structural information has been obtained which has led to specific models of protein structure in the membrane (Engelman et al., 1982; Huang et al., 1982; Agard & Stroud, 1982). The retinal chromophore of bacteriorhodopsin is boun...
متن کاملMolecular dynamics study of the proton pump cycle of bacteriorhodopsin.
Retinal isomerization reactions, which are functionally important in the proton pump cycle of bacteriorhodopsin, were studied by molecular dynamics simulations performed on the complete protein. Retinal isomerizations were simulated in situ to account for the effects of the retinal-protein interactions. The protein structure employed was that described in Nonella et al. [Nonella, M., Windemuth,...
متن کاملLeptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote.
Bacteriorhodopsin-like proteins provide archaea and eubacteria with a unique bioenergetic pathway comprising light-driven transmembrane proton translocation by a single retinal-binding protein. Recently, homologous proteins were found to perform photosensory functions in lower eukaryotes, but no active ion transport by eukaryotic rhodopsins was detected. By demonstrating light-driven proton pum...
متن کاملSchiff Base Switch II Precedes the Retinal Thermal Isomerization in the Photocycle of Bacteriorhodopsin
In bacteriorhodopsin, the order of molecular events that control the cytoplasmic or extracellular accessibility of the Schiff bases (SB) are not well understood. We use molecular dynamics simulations to study a process involved in the second accessibility switch of SB that occurs after its reprotonation in the N intermediate of the photocycle. We find that once protonated, the SB C15 = NZ bond ...
متن کاملEffect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.
The retinylidene chromophore mutant (Y185F) of bacteriorhodopsin, in which Tyr-185 is substituted by phenylalanine, is examined and compared with wild-type bacteriorhodopsin expressed in Escherichia coli; both were reinstituted similarly in vesicles. The Y185F mutant shows (at least) two distinct spectra at neutral pH. Upon light absorption, the blue species (which absorbs in the red) behaves a...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2001
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.41.s9_2