Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin.

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Journal of Molecular Biology

• Publication date

  2000-07-28

• Fields of study

  Biology, Medicine, Physics, Chemistry

• Identifiers
  DOI 10.1006/JMBI.2000.3884PMID 10903866
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin.

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  1999cited by this paper
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  1999influential reference
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  1999cited by this paper
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  1999influential reference
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  1999cited by this paper
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• The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH.

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  1998cited by this paper
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  1998influential reference
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• Proton translocation by bacteriorhodopsin and heme-copper oxidases.

  1998cited by this paper
• Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface.

  1998cited by this paper
• Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle.

  1998cited by this paper
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  1998influential reference
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  1998cited by this paper
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  1997cited by this paper
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• Mechanism of Ion Transport across Membranes

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  1997cited by this paper
• Infrared Difference Spectra of the Intermediates L, M, N, and O of the Bacteriorhodopsin Photoreaction Obtained by Time-Resolved Attenuated Total Reflection Spectroscopy

  1997cited by this paper
• Time-resolved fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin.

  1997cited by this paper
• Evidence for the first phase of the reprotonation switch of bacteriorhodopsin from time-resolved photovoltage and flash photolysis experiments on the photoreversal of the M-intermediate.

  1997cited by this paper
• General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model.

  1997cited by this paper
• X‐Ray Diffraction Studies of Bacteriorhodopsin. Determination of the Positions of Mercury Label at Several Engineered Cysteine Residues

  1997cited by this paper
• The tertiary structural changes in bacteriorhodopsin occur between M states: X‐ray diffraction and Fourier transform infrared spectroscopy

  1997cited by this paper
• Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle.

  1996cited by this paper
• Lipidic cubic phases: a novel concept for the crystallization of membrane proteins.

  1996cited by this paper
• Determination of the transiently lowered pKa of the retinal Schiff base during the photocycle of bacteriorhodopsin.

  1996influential reference
• A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition.

  1996cited by this paper
• Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.

  1996cited by this paper
• Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 13-cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle.

  1996cited by this paper
• Electron-crystallographic refinement of the structure of bacteriorhodopsin.

  1996cited by this paper
• Hydrogen bonds of water and C==O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin.

  1996cited by this paper
• Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.

  1996cited by this paper
• Complicated character of the M decay pH dependence in the D96N mutant is due to the two pathways of the M conversion

  1996cited by this paper
• Interaction of proton and chloride transfer pathways in recombinant bacteriorhodopsin with chloride transport activity: implications for the chloride translocation mechanism.

  1996cited by this paper
• Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release.

  1996cited by this paper
• A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin.

  1996cited by this paper
• Interaction of tryptophan-182 with the retinal 9-methyl group in the L intermediate of bacteriorhodopsin.

  1995cited by this paper
• The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.

  1995cited by this paper
• Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin (*)

  1995influential reference
• Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.

  1995cited by this paper
• Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle.

  1995cited by this paper
• Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle.

  1995cited by this paper
• Structure and Function of Halorhodopsin

  1995cited by this paper
• The Photocycles of Bacteriorhodopsin

  1995cited by this paper
• pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy.

  1994cited by this paper
• Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study.

  1994cited by this paper
• The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues.

  1994influential reference
• Complete identification of C = O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin.

  1994influential reference
• The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.

  1994influential reference
• Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction.

  1994cited by this paper
• Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 1. Proton migration along the surface of bacteriorhodopsin micelles and its delayed transfer from surface to bulk.

  1994cited by this paper
• Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles.

  1994cited by this paper
• Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle.

  1994cited by this paper
• The bacteriorhodopsin photocycle: direct structural study of two substrates of the M-intermediate.

  1994cited by this paper
• Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin.

  1994cited by this paper
• Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

  1993cited by this paper
• Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change.

  1993cited by this paper
• Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle.

  1993cited by this paper
• Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure.

  1992influential reference
• THE TWO CONSECUTIVE M SUBSTATES IN THE PHOTOCYCLE OF BACTERIORHODOPSIN ARE AFFECTED SPECIFICALLY BY THE D85N AND D96N RESIDUE REPLACEMENTS

  1992cited by this paper
• Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy.

  1992cited by this paper
• Pathways of proton release in the bacteriorhodopsin photocycle.

  1992cited by this paper
• Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle.

  1992cited by this paper
• Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization.

  1991cited by this paper
• Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base.

  1991influential reference
• Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation.

  1991influential reference
• Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition.

  1991cited by this paper
• Fourier transform infrared study of the N intermediate of bacteriorhodopsin.

  1991cited by this paper
• Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin.

  1991cited by this paper
• Thermodynamics and energy coupling in the bacteriorhodopsin photocycle.

  1991cited by this paper
• Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle.

  1991cited by this paper
• The role of back-reactions and proton uptake during the N----O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study.

  1990cited by this paper
• Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?

  1990cited by this paper
• Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.

  1989cited by this paper
• Role of aspartate-96 in proton translocation by bacteriorhodopsin.

  1989cited by this paper
• Bacteriorhodopsin's L550 intermediate contains a C14-C15 s-trans-retinal chromophore.

  1988cited by this paper
• Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanism.

  1988cited by this paper
• Kinetic resonance Raman studies reveal different conformational states of bacteriorhodopsin.

  1988cited by this paper
• Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. M412 and L550 intermediates.

  1987cited by this paper
• Are C14-C15 single bond isomerizations of the retinal chromophore involved in the proton-pumping mechanism of bacteriorhodopsin?

  1986cited by this paper
• TIME‐RESOLVED RESONANCE RAMAN STUDIES ON THE PHOTOCHEMICAL CYCLE OF BACTERIORHODOPSIN

  1986cited by this paper
• The effect of protonation and electrical interactions on the stereochemistry of retinal schiff bases.

  1985cited by this paper

• Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography

  2025cites this paper
• Bacteriorhodopsin proton-pumping mechanism: successes and challenges in computational approaches.

  2025cites this paper
• Intracellular microbial rhodopsin-based optogenetics to control metabolism and cell signaling.

  2024cites this paper
• Structural studies of bacteriorhodopsin in BC era

  2023cites this paper
• Transmembrane proteins—Different anchoring systems

  2023cites this paper
• Voltage Imaging with Engineered Proton-Pumping Rhodopsins: Insights from the Proton Transfer Pathway

  2023cites this paper
• Protein dynamics of a light-driven Na+ pump rhodopsin probed using a tryptophan residue near the retinal chromophore

  2023cites this paper
• Common mechanism of activated catalysis in P-loop fold nucleoside triphosphatases - in varietate concordia

  2022cites this paper
• Light-driven proton transfers and proton transport by microbial rhodopsins - A biophysical perspective.

  2022cites this paper
• Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases—United in Diversity

  2022cites this paper
• Archaeal Lipids Regulating the Trimeric Structure Dynamics of Bacteriorhodopsin for Efficient Proton Release and Uptake

  2022cites this paper
• Photoreaction Pathways of Bacteriorhodopsin and Its D96N Mutant as Revealed by in Situ Photoirradiation Solid-State NMR

  2022cites this paper
• Application of direct electrometry in studies of microbial rhodopsins reconstituted in proteoliposomes

  2022cites this paper
• Quantum-Mechanical Molecular Dynamics Simulations on Secondary Proton Transfer in Bacteriorhodopsin Using Realistic Models.

  2021cites this paper
• Directional Proton Conductance in Bacteriorhodopsin Is Driven by Concentration Gradient, Not Affinity Gradient

  2021cites this paper
• Dynamic Coupling of Tyrosine 185 with the Bacteriorhodopsin Photocycle, as Revealed by Chemical Shift Assisted AF-QM/MM Calculations and Molecular Dynamic Simulations

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• Functional Mechanism of Proton Pump-Type Rhodopsins Found in Various Microorganisms as a Potential Effective Tool in Optogenetics

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  2019cites this paper
• Bacteriorhodopsin: Structural Insights Revealed Using X-Ray Lasers and Synchrotron Radiation.

  2019cites this paper
• Unusual features of the c-ring of F1FO ATP synthases

  2019cites this paper
• Photoreaction pathways and photointermediates of retinal-binding photoreceptor proteins as revealed by in situ photoirradiation solid-state NMR spectroscopy

  2019cites this paper
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  2018cites this paper
• In Situ Photo Irradiation Solid-State NMR Spectroscopy Applied to Retinal-Binding Membrane Proteins

  2018cites this paper
• Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle as revealed by in situ spectroscopic studies.

  2018cites this paper
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  2017cites this paper
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  2016cites this paper
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  2016cites this paper
• A three-dimensional movie of structural changes in bacteriorhodopsin

  2016cites this paper
• Light‐Activated Reversible Imine Isomerization: Towards a Photochromic Protein Switch

  2016cites this paper
• Ion-pumping microbial rhodopsins

  2015cites this paper
• Bacteriorhodopsin: Would the real structural intermediates please stand up?

  2015influential citation
• Vibrational spectroscopy of an optogenetic rhodopsin: a biophysical study of molecular mechanisms

  2015cites this paper
• Conversion of a light-driven proton pump into a light-gated ion channel

  2015cites this paper
• Proton Transfers in a Channelrhodopsin-1 Studied by Fourier Transform Infrared (FTIR) Difference Spectroscopy and Site-directed Mutagenesis*

  2015cites this paper
• Dynamic regulation of lipid-protein interactions.

  2015cites this paper
• Characterization of photo-intermediates in the photo-reaction pathways of a bacteriorhodopsin Y185F mutant using in situ photo-irradiation solid-state NMR spectroscopy

  2015cites this paper
• ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

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• The role of protein-bound water molecules in microbial rhodopsins.

  2014cites this paper
• Infrared spectral marker bands characterizing a transient water wire inside a hydrophobic membrane protein.

  2014cites this paper
• Proton-Pumping Microbial Rhodopsins – Ubiquitous Structurally Simple Helpers of Respiration and Photosynthesis

  2014cites this paper
• Stable Closure of the Cytoplasmic Half-Channel Is Required for Efficient Proton Transport at Physiological Membrane Potentials in the Bacteriorhodopsin Catalytic Cycle

  2014cites this paper
• Water Structural Changes in the L and M Photocycle Intermediates of Bacteriorhodopsin as Revealed by Time-Resolved Step-Scan FTIR Spectroscopy +

  2014cites this paper
• Hybrid quantum-classical study of the non-adiabatic cis-trans photoisomerization in a model polyatomic molecule

  2014cites this paper
• The role of protein-boundwater molecules inmicrobial rhodopsins ☆ , ☆ ☆

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• Title Schiff Base Switch II Precedes the Retinal Thermal Isomerization in the Photocycle of Bacteriorhodopsin Permalink

  2013cites this paper
• Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

  2013cites this paper
• Schiff Base Switch II Precedes the Retinal Thermal Isomerization in the Photocycle of Bacteriorhodopsin

  2013cites this paper
• Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.

  2013cites this paper
• Crystal structure of the O intermediate of the Leu93→Ala mutant of bacteriorhodopsin

  2012cites this paper
• Optical applications of biomolecules

  2012cites this paper
• Multi-species biclustering: An integrative method to identify functional gene conservation between multiple species

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• Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

  2012cites this paper
• 8.10 Light Capture and Energy Transduction in Bacterial Rhodopsins and Related Proteins

  2012cites this paper
• Photochemical characterization of a novel fungal rhodopsin from Phaeosphaeria nodorum.

  2011cites this paper
• Proton transfer via a transient linear water-molecule chain in a membrane protein

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• X-ray-radiation-induced changes in bacteriorhodopsin structure.

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• Suppressed or recovered intensities analysis in site-directed (13)C NMR: assessment of low-frequency fluctuations in bacteriorhodopsin and D85N mutants revisited.

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• Water Pathways in the Bacteriorhodopsin Proton Pump

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  2009cites this paper
• Structural changes in the N and N' states of the bacteriorhodopsin photocycle.

  2009cites this paper
• Protein Conformational Changes in the Bacteriorhodopsin Photocycle: Comparison of Findings from Electron and X-Ray Crystallographic Analyses

  2009cites this paper
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  2009cites this paper
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  2009cites this paper
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  2008cites this paper
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  2008cites this paper
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  2008cites this paper
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  2008cites this paper
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  2008cites this paper
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  2008cites this paper
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  2008cites this paper
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  2007cites this paper
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  2007cites this paper
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  2007cites this paper
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  2007cites this paper
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• [Photochemical properties of a bacteriorhodopsin analogue containing 13-desmethyl-13-(trifluoromethyl)retinal].

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