The structure and mechanism of the family of retinal proteins from halophilic archaea
Current Opinion in Structural BiologyPublished 1 August 1998
Dieter Oesterhelt
Citations274
SJR quartileQ1
SJR score2.91
SNIP1.48
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TL;DR
Experimental modulation of the vectoriality and ion specificity by altering the substrate availability, point mutations and light conditions for the different retinal proteins allows the proposal of a general model of ion transport for this protein family.
Abstract
Retinal proteins from halophilic archaea provide a unique opportunity to analyze vectorial ion translocation. Studies on its structure, conformational changes, proton conduction and electrogenic steps have helped to elucidate the catalytic cycle of bacteriorhodopsin in increasing detail. Experimental modulation of the vectoriality and ion specificity by altering the substrate availability, point mutations and light conditions for the different retinal proteins allows the proposal of a general model of ion transport for this protein family.
Keywords
ChemistryNeuroscienceBiochemistry, Genetics and Molecular Biology
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34 Citations1998Hans Jürgen Sass, R. Gessenich +5 more
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The lack of intermediates N and O demonstrated that the M state did not undergo a change from the extracellular to the cytoplasmic conformation (M1 to M2 transition), as already indicated by Fourier transform infrared spectroscopy, quasielastic incoherent neutron scattering, and electric signal measurements described in the literature.
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Biophysical JournalHis166 is critical for active-site proton transfer and phototaxis signaling by sensory rhodopsin I
22 Citations1997Xue Nong Zhang, John L. Spudich
The conclusions are that His166 plays a role in the pathways of proton transfer both to and from the Schiff base in the SRI-Htrl complex, either as a structurally important residue or possibly as a participant in proton transfers, and is involved in the modulation of SRI photoreaction kinetics by Htrl.
The Journal of Physical Chemistry AAnalysis of the Excited-State Dynamics of 13-<i>trans</i>-<i>locked</i>-Bacteriorhodopsin
20 Citations1997Ryo Akiyama, Akira Yoshimori +4 more
The excited-state dynamics of 13-trans-locked-bacteriorhodopsin appears globally quite similar to that of native bacteriorhodopin up to about 100 fs, and the difference of them becomes slightly evident after 100 fs up t...
Physica B Condensed MatterNeutron diffraction on purple membranes essential water molecules in the light-driven proton pump bacteriorhodopsin
17 Citations1997Thomas Hauß, Γεώργιος Παπαδόπουλος +3 more
BiochemistryThreonine-89 Participates in the Active Site of Bacteriorhodopsin: Evidence for a Role in Color Regulation and Schiff Base Proton Transfer
16 Citations1997Terence Stephen Russell, Matthew A. Coleman +3 more
Evidence is found that Thr-89 also participates in this active site which participates in proton transfers and regulates the visible absorption of bacteriorhodopsin and its photointermediates and the properties of the 13-cis retinylidene chromophore of dark-adapted T 89N as well as the K and L intermediates of the T89N photocycle are similar to the wild-type bacteriorodopsin.
BiochemistryTime-Resolved Titrations of ASP-85 in Bacteriorhodopsin: The Multicomponent Kinetic Mechanism
14 Citations1997Noga Friedman, Itay Rousso +5 more
Analysis of the data over a range of cation concentrations and pH values leads to the conclusion that the rate-determining step in the overall titration of Asp-85 is proton translocation through a specific proton channel.
FEBS LettersSimilarity of bacteriorhodopsin structural changes triggered by chromophore removal and light‐driven proton transport
13 Citations1997G. Ludlam, Kenneth J. Rothschild
Evidence that similar conformational changes occur upon removal of the retinylidene chromophore of bacteriorhodopsin to form the apoprotein bacterioopsin (bO) suggests a simple ligand‐binding model of proton transport in bacteriorodopsin which may have relevance to other transport and signal transducing membrane proteins including the visual photoreceptor rhodopsins.
BiochemistryTime-Resolved Titrations of the Schiff Base and of the Asp85 Residue in Artificial Bacteriorhodopsins
13 Citations1995S. Druckmann, Michael Ottolenghi +3 more
The Schiff base is titrable from the outside medium via a proton channel, which becomes saturated, and thus rate determining, below pH approximately equal to 7, and found that this is the case for the Schiff base in the pH range between 7 and 9 but not at lower pH.
Protein Engineering Design and SelectionThree-dimensional model of sensory rhodopsin I reveals important restraints between the protein and the chromophore
13 Citations1997Shin-Jen Lin, Bing Yan
A structural model is constructed for the integral membrane protein, sensory rhodopsin I (SRI), the phototaxis receptor of the archaeon Halobacterium salinarium, and it is hypothesized that conformational changes of the protein provide the signal recognized by the transducer.
Photochemistry and PhotobiologyMutation of Arginine 134 to Lysine Alters the pK<sub>a</sub>s of Key Groups Involved in Proton Pumping by Bacteriorhodopsin
12 Citations1997Saurav Misra, Charles H. Martin +5 more
The pH dependence of M formation is explained as being due to titration of the counter‐ion, D85, and of the proton release group, which is located near the extracellular surface of bacteriorhodopsin (bR) and may interact with one or more nearby glutamate residues.
Signal Transduction in Halobacteria
11 Citations1989Dieter Oesterhelt, Wolfgang Marwan
The search for photosynthetically efficient green light and the avoidance of inefficient blue light or lethal ultra-violet light allows halobacteria to survive by means of photosynthesis in a natural habitat of brines and salt ponds under strong sunlight.
Solid State IonicsThe role of the surface group in funnelling of protons towards the protonic channel of bacteriorhodopsin
10 Citations1997Esther Nachliel, Sharon Yaniv-Checover +1 more
Observations indicate that the surface of the protein had evolved as a functional element in directing the substrate towards the active site in proton transfer between the bulk and an indicator.
Proteins Structure Function and BioinformaticsModeling of halorhodopsin and rhodopsin based on bacteriorhodopsin
9 Citations1996Martin Neumüller, Fritz Jähnig
The results indicate that even for a nonhomologous, but structurally related, protein such as Rh, an acceptable model structure can be derived from the structure of BR.
BiochemistryInteraction between Asp-85 and the Proton-Releasing Group in Bacteriorhodopsin. A Study of an O-like Photocycle Intermediate
8 Citations1997Y. Gat, Noga Friedman +2 more
The O1 species of pigments I and II are identified as an unusually long-lived (all-trans) intermediate of the photocycle of their 13-cis isomer, and the pKa values are determined and discussed in relation to those pertaining to the unphotolyzed (dark-adapted) pigments.
Pure and Applied ChemistryOn the molecular origin of the protein catalysis of the primary process in bacteriorhodopsin photosynthesis: Retinal photoisomerization
7 Citations1997Mostafa A. El‐Sayed, Stephan L. Logunov
BiochemistryInvestigation of the Proton Release Channel of Bacteriorhodopsin in Different Intermediates of the Photo Cycle. A Molecular Dynamics Study
6 Citations1997Jochen Nagel, Olle Edholm +2 more
Molecular dynamics simulations on bacteriorhodopsin were performed starting from a conformation based on electron cryomicroscopy studies and it is concluded that the guanidinium group of Arg82 is located close to the Schiff base and stays there at least up to the M-intermediate of the photocycle.
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