TY - JOUR. T1 - Effect of Asp85 replacement by Thr on the conformation, surface electric properties and stability of bacteriorhodopsin. AU - Taneva, Stefka G.. AU - Gõi, Felix M.. AU - Tuparev, Nikolai P.. AU - Petkanchin, Ivana. AU - Dér, A.. AU - Muga, Arturo. PY - 2002/9/25. Y1 - 2002/9/25. N2 - The role of Asp85 in maintaining bacteriorhodopsin structure has been analyzed by infrared spectroscopy, electric light scattering and differential scanning calorimetry. In comparison with the wild type bacteriorhodopsin, the mutant protein D85T shows a different conformation, electric dipole moments and decreased thermal stability. The conformational rearrangements affect both the transmembrane helices and the extramembranous protein segments. Both electric dipoles - the permanent dipole moment and the electric polarizability - have drastically lower values for the membranes containing D85T variant of bacteriorhodopsin. Therefore, this single amino acid mutation not only changes bacteriorhodopsin ...

The primary processes of the photochemical cycle of light-adapted bacteriorhodopsin (BR) were studied by various experimental techniques with a time resolution of 5 × 10-13 s. The following results were obtained. (a) After optical excitation the first excited singlet state S1 of bacteriorhodopsin is observed via its fluorescence and absorption properties. The population of the excited singlet state decays with a lifetime τ1 of ~0.7 ps (430 ± 50 fs) (52). (b) With the same time constant the first ground-state intermediate J builds up. Its absorption spectrum is red-shifted relative to the spectrum of BR by ~30 nm. (c) The second photoproduct K, which appears with a time constant of τ2 = 5 ps shows a red-shift of 20 nm, relative to the peak of BR. Its absorption remains constant for the observation time of 300 ps. (d) Upon suspending bacteriorhodopsin in D2O and deuterating the retinal Schiff base at its nitrogen (lysine 216), the same photoproducts J and K are observed. The relaxation time ...

The vibrational dynamics of the retinal chromophore all-trans-to-13-cis photoisomerization in bacteriorhodopsin has been studied with mid-infrared absorption spectroscopy at high time resolution (about 200 femtoseconds). After photoexcitation of light-adapted bacteriorhodopsin, the transient infrared absorption was probed in a broad spectral region, including vibrations with dominant C-C, C=C, and C=NH stretching mode amplitude. All photoproduct modes, especially those around 1190 reciprocal-centimeters that are indicative for a 13-cis configuration of the chromophore, rise with a time constant of ∼0.5 picosecond. The results presented give direct vibrational-spectroscopic evidence for the isomerization taking place within 0.5 picosecond, as has been suggested by previous optical femtosecond time-resolved experiments but questioned recently by picosecond time-resolved vibrational spectroscopy experiments. ...

Chemical exchange of hydrogen atoms is the basis for many biological processes, including energy conversion from light into chemical potentials. In a recent collaborative study of the SFB 1078 under the direction of Hartmut Oschkinat (B1), Peter Hegemann (B1, B2) and Roland R. Netz (C1), proton exchange was detected and characterized in the light-driven proton pump bacteriorhodopsin, a well-established model system for protonation dynamics studies. The work, published in the new open access journal Communications Biology of the Nature Publishing Group, revealed that reversible proton translocation occurs even in the dark-state of the protein, involving the retinal Schiff base and D85 exchanging protons with H2O. The authors find evidence of an active site proton cage and possible proton transfer via R82. The experimental observations have been corroborated by theoretical approaches, further extending the general understanding of proton exchange in proteins.. Friedrich, D., Brünig, F. N., ...

Biological molecules and assemblies, such as the photochemical reaction center, are capable of capturing light with good quantum efficiency and transforming it into chemical energy. If properly exploited, such assemblies have potential applications as biomolecule information processing units.. Bacteriorhodopsin, from the purple membrane bacterium Halobacterium halobium, is one such system that has been studied extensively and has been commercialized into optical holographic memories (Birge 1995). In the bacterium, the protein bacteriorhodopsin self-assembles into ordered lipid patches. The protein absorbs light and undergoes a cycle involving a complex series of intermediates, resulting in a proton being pumped across the membrane. It was information developed from understanding the basic science behind the way that bacteriorhodopsin works that led to the use of bacteriorhodopsin as a biomolecule information processing unit. To be used for information storage, the protein is placed under ...

Th?e atomic structure of the light-driven ion pump bacteriorhodopsin and the surrounding lipid matrix was determined by X-ray diffraction of crystals grown in cubic lipid phase. In the extracellular region, an extensive three-dimensional hydrogen-bonded network of protein residues and seven water mo …

The transmembrane electrochemical proton gradient is a key source of cellular energy. Bacteriorhodopsin (bR), the simplest and most studied proton pump, moves protons from low to high concentration by harnessing light energy, creating the transmembrane el

1DZE: Crystal Structure of the M Intermediate of Bacteriorhodopsin: Allosteric Structural Changes Mediated by Sliding Movement of a Transmembrane Helix

Heyes CD, EL-Sayed MA. Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization. Biophysical journal [Internet]. 2003 ;85(1):426-434. Available from: http://dx.doi.org/10.1016/S0006-3495(03)74487-7 ...

SWISS-MODEL Template Library (SMTL) entry for 5h2l.1. A three dimensional movie of structural changes in bacteriorhodopsin: structure obtained 5.25 us after photoexcitation

3-Fluoro-DL-tyrosine can be used to study how halogenated tyrosines affect proteins such as bacteriorhodopsin, microvillar enzymes, and β-galactosidases.

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Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mutant, at the resolution of 2.5 Å. While the HmBRI retinal-binding pocket and proton donor site are similar to those of other archaeal proton pumps, its proton release region is extended and contains additional water molecules. The proteins fold is reinforced by three novel inter-helical hydrogen bonds, two of which result from double substitutions relative to Halobacterium salinarum bacteriorhodopsin and other similar proteins. Despite the expression in Escherichia coli and consequent absence of native lipids, the protein assembles as a trimer in crystals. The unique extended loop between the helices D and E of HmBRI makes contacts with the adjacent protomer and appears to stabilize the interface. Many lipidic hydrophobic tail groups are discernible in the

A substantial number of spontaneous bacterio-opsin mutants of Halobacterium halobium are the result of insertion elements up to 1400 bp upstream of the bacterio-opsin (bop) gene. The nucleotide sequence of 1800 bp upstream of the bop gene has been determined. There is a 1118 bp open reading frame (ORF) located within this region which is transcribed and which coincides with the distribution of insertion elements upstream of the bop gene in Bop mutants. Therefore, we propose that there is a gene (brp gene) 526 bp upstream of the bop gene. This putative gene is transcribed in the opposite direction as the bop gene and could encode a protein of 37,500 D (359 amino acids) with a codon usage similar to bacterio-opsin. The 5 terminus of the brp transcript has been determined. The brp transcript and the bop mRNA are complementary for 13 residues near their 5 termini and both transcripts start at or near the initiating codon of the gene. Both transcripts could form similar hairpin loop structures at ...

Biological light-driven proton pumps use light to move protons across a cell membrane, creating a proton gradient. Although photochromic compounds such as spiropyrans can reversibly convert between two structures with differing pKa values, spiropyrans have not been used to generate either a light-driven proton pump or an electrical current. Here, we report an artificial light-harvesting system based on a supported liquid membrane doped with a spiropyran. Irradiating the membrane with ultraviolet light induces a ring-opening reaction, converting spiropyran to merocyanine, whereas irradiation with visible light induces the reverse reaction. When the membrane is irradiated with ultraviolet and visible light on opposite sides, H+ is taken up by merocyanine, carried through the polymeric membrane and released on the other side. We show that this system produces a light-induced proton flux, an electrical current with an efficiency of ~0.12%, an open-circuit voltage of ~210 mV and a membrane gradient of ~3.6

Heyes CD, Wang J, Sanii LS, EL-Sayed MA. Fourier transform infrared study of the effect of different cations on bacteriorhodopsin protein thermal stability. Biophysical journal [Internet]. 2002 ;82(3):1598-1606. Available from: http://dx.doi.org/10.1016/S0006-3495(02)75511-2 ...

0070]Bacteriorhodopsin (purple membrane) has been incorporated in liposomes using sonication. The lipid mixture used was 4:1 DOPE: EggPC. DOPE has been shown to increase the incorporation of bacteriorhodopsin (bR). 10 mM pH buffer was used so that we could see the change in pH due to bacteriorhodopsin. After gelation, a few drops of buffer were added to the sample if the pH was not stable, for example due to improper contact with the pH electrode. The pH levels of gels containing the bR-incorporated lipsomes before and after light exposure were measured and compared with the pH levels of blank-liposomes in gel before and after light exposure. Light with a yellow light filter was shined for 30 sec and a break for 60 sec was given. This was due to the fact that the blank-liposome gel in buffer was showing a slight decrease in pH, which was suspected to be due to a heat effect. The pH levels of the blank returned to baseline after exposure to light, whereas the pH levels of the bR-incorporated ...

The story behind optogenetics is a story of convergence of two seemingly unrelated fields: microbial microbiology and neuroscience. In 1971, Walther Stoeckenius and Dieter Oesterhelt discovered the transmembrane protein bacteriorhodopsin (BR) that is capable of moving ions in the presence of light. BR is highly expressed in haloarcheal membranes while a similar transmembrane protein proteorhodopsin (PR) is expressed in eubacteria. In 1977, Matsuno-Yagi and Mukohata described the ion pump channel halorhodopsin which displaces extracellular chloride ions in to the cell. As these discoveries were happening in the background, a growing desire to effectively control the neurons was ever -prevalent. During this period, neuroscientist adopted the idea that cognitive processes were distributed in various localizations of the cortex. This fact evident when lesions in specific areas would lead to loss of a specific process. Even fMRIs and PET solidified this point, but, even with these high-tech ...

The story behind optogenetics is a story of convergence of two seemingly unrelated fields: microbial microbiology and neuroscience. In 1971, Walther Stoeckenius and Dieter Oesterhelt discovered the transmembrane protein bacteriorhodopsin (BR) that is capable of moving ions in the presence of light. BR is highly expressed in haloarcheal membranes while a similar transmembrane protein proteorhodopsin (PR) is expressed in eubacteria. In 1977, Matsuno-Yagi and Mukohata described the ion pump channel halorhodopsin which displaces extracellular chloride ions in to the cell. As these discoveries were happening in the background, a growing desire to effectively control the neurons was ever -prevalent. During this period, neuroscientist adopted the idea that cognitive processes were distributed in various localizations of the cortex. This fact evident when lesions in specific areas would lead to loss of a specific process. Even fMRIs and PET solidified this point, but, even with these high-tech ...

1BCT: Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution.

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Parent Directory - phylogenetictree.jpg 20-Jul-2014 00:42 24K phylogenetictree-t.jpg 20-Jul-2014 00:42 7.0K Bacteriorhodopsin/ 20-Jul-2014 00:42 - Archaeacells.htm 20-Jul-2014 00:42 965 ...

Last replication packet received at 2021-09-17T02:01:05Z. Brought to you by MetaBrainz Foundation and our sponsors and supporters. Cover Art provided by the Cover Art Archive. ...

https://inspirehep.net/literature/892684 Inspire Record 892684 DOI 10.17182/hepdata.62222 https://doi.org/10.17182/hepdata.62222 We study the processes e+e- --, K+ K- pi+pi-gamma, K+ K- pi0pi0gamma, and K+ K- K+ K-gamma, where the photon is radiated from the initial state. About 84000, 8000, and 4200 fully reconstructed events, respectively, are selected from 454 fb-1 of BaBar data. The invariant mass of the hadronic final state defines the \epem center-of-mass energy, so that the K+ K- pi+pi- data can be compared with direct measurements of the e+e- --, K+ K- pi+pi- reaction. No direct measurements exist for the e+e- --, K+ K-pi0pi0 or e+e- --, K+ K-K+ K- reactions, and we present an update of our previous result with doubled statistics. Studying the structure of these events, we find contributions from a number of intermediate states, and extract their cross sections. In particular, we perform a more detailed study of the e+e- --, phi(1020)pipigamma reaction, and confirm the presence of the ...

Die Erfindung betrifft einen Testträger zur analytischen Bestim mung eines Bestandteils einer Körperflüssigkeit mit einer Basis schicht und mindestens zwei flachen im Ausgangszustand des Test trägers vor Durchführung einer Bestimmung voneinander getrennten, jedoch durch externe Manipulation in Kontakt zueinander bringbaren Testschichten. The invention relates to a test carrier for the analytical Bestim mung a component of a body fluid with a base layer and at least two flat in the initial state of the test carrier prior to making a determination on separate, but mutually by external manipulation can be brought into contact test layers. Während früher im klinischen Labor die Konzentration beispiels weise der Bestandteile des Blutes praktisch ausschließlich mit Hilfe flüssiger Reagenzien bestimmt wurde, haben in jüngerer Zeit sogenannte trägergebundene Tests zunehmend an Bedeutung gewonnen. While earlier in the clinical laboratory, the concentration example, the components of the blood ...

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A group of microbial retinal proteins most closely related to the proton pump xanthorhodopsin has a novel sequence motif and a novel function. Instead of, or in addition to, proton transport, they perform light-driven sodium ion transport, as reported for one representative of this group (KR2) from Krokinobacter. In this paper, we examine a similar protein, GLR from Gillisia limnaea, expressed in Escherichia coli, which shares some properties with KR2 but transports only Na +. The absorption spectrum of GLR is insensitive to Na + at concentrations of ≤3 M. However, very low concentrations of Na + cause profound differences in the decay and rise time of photocycle intermediates, consistent with a switch from a Na +-independent to a Na +-dependent photocycle (or photocycle branch) at ~60 μM Na +. The rates of photocycle steps in the latter, but not the former, are linearly dependent on Na + concentration. This suggests that a high-affinity Na + binding site is created transiently after ...

In a general description of the various ion transport modes found for halobacterial retinal proteins (Haupts et al., 1997), the transport mechanism is represented by a sequence of six principal reaction steps: retinal isomerization to 13‐cis or all‐trans (either photochemical, designated as I*, or thermal, I), ion translocation to or from the Schiff base (T) and switch of the Schiff base accessibility towards the EC or CP side (S). Within this framework, the anion transport mechanism of wild type HR, taking into consideration the results on specific mutants, can be described as follows (Figure 7): in the initial state, the substrate anion occupies a binding site constituted by R108 and T111, also interacting with the protonated Schiff base (Walter and Braiman, 1994), and the Schiff base is accessible for ions from the EC side. (1) Light‐induced isomerization (I*) is followed by (2) translocation of this anion towards the Schiff base (T), where it is located in the HR520 intermediate state ...

Author: Laso-Pérez, R. et al.; Genre: Journal Article; Published in Print: 2016-11-17; Open Access; Keywords: Archaeal physiology; Metabolomics; Environmental microbiology|br/|; Title: Thermophilic archaea activate butane via alkyl-coenzyme M formation.

Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. The enzyme activity was completely and irreversibly lost if the NaCl concentration fell below 2 M. The protease consists of one polypeptide chain with a molecular weight of 41,000. It is characteristically enriched in Asx and Glx content, whereas the level of basic amino acids in the enzyme molecule is unusually low. The protease shows a preference for leucine in the carboxylic side of the scissile bond of the substrate, cleaving the B-chain of oxidized bovine insulin only at the Leu15-Tyr16 bond and liberating p-nitroaniline from L-pyroglutamyl-L-alanyl-L-alanyl-L-leucine-p-nitroanilide. ...

Molecular organization and dynamics in protein-rich membranes have been studied by investigating transport (diffusion-concentration product) of molecular oxygen at various locations in reconstituted membranes of bacteriorhodopsin (BR) and L-alpha-dimyristoylphosphatidylcholine. Oxygen transport was evaluated by monitoring the bimolecular collision of molecular oxygen with four types of nitroxide lipid spin labels placed at various locations in the membrane. The collision rate was estimated from the spin-lattice relaxation times (T1s) measured at various oxygen partial pressures by analyzing the short-pulse saturation recovery ESR signals. CD spectra and decay of polarized flash-induced photodichroism of bacteriorhodopsin indicated that BR molecules are monomers in reconstituted membranes with a lipid/BR molar ratio of 80 (80-rec) and are 25% monomers and 75% trimers plus oligomers of trimers when the lipid/BR ratio is 40 (40-rec). In the 80-rec, the lipid environment is homogeneous on a ...

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The flagship monthly journal of SPIE, |i|Optical Engineering|/i| (OE) publishes peer-reviewed papers reporting on research and development in all areas of optics, photonics, and imaging science and engineering.

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The protonation state of embedded charged residues in transmembrane proteins (TMPs) can control the onset of protein function. It is understood that interactions between an embedded charged residue and other charged or polar residues in the moiety would influence its pKa, but how the surrounding environment in which the TMP resides affects the pKa of these residues is unclear.

Worcester Polytechnic Institute (WPI) and Quinsigamond Community College (QCC) have been awarded a $4 million grant by the Commonwealth of Massachuset

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A post-doctoral position is available immediately in the laboratory of Dr Joe Cockburn, at the Astbury Centre, University of Leeds, UK to perform structure-function studies on ciliary proteins.. The position is funded by The Wellcome Trust and is available immediately for a period of 24 months. The start date is flexible but must be before September 2017.. The deadline for applications is Monday 16th January 2017.. More information about the position and how to apply can be found here. ...

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In thermodynamic, an irreversible process is defined as a process that cannot be reversed, the process cannot return both the system and the surroundings to their original conditions. During irreversible process, the entropy of the system increases rapidly and it cannot be reduced back to its initial value. During the irreversible process the various states of the system on the path of change from initial state to final state are not in equilibrium with each other. There are many factors that make a process irreversible, they include:. ...

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