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 ...
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 ...
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
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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Classical planning is the problem of finding a sequence of actions, from a given initial state to some goal state. While, in generalized planning, a plan is a solution to a set of planning problems, which belong to the ...
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
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 ...
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 ...
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 ...
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. ...
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.
Adrenodoxin, Escherichia Coli, Kinetics, Molecular Cloning, Point Mutation, Polymerase Chain Reaction, Protein Binding, Recombinant Proteins, Structure-Activity ...
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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Sensing light from the environment using photoreceptors is of great adaptive significance to eukaryotes. A prominent feature of the photochemistry of these receptors is the photocycle length, the time taken to decay from the initial signaling light state back to the receptive dark state. Photoreceptors have distinct photocycle lengths and this suggests evolutionary selection of the photochemistry for biological function. However, the biological significance of the photocycle length is not understood as most in vivo studies with photoreceptors utilize true null or blind photoreceptor mutants. Neurospora crassa provides a fantastic template for studying photobiology and the plethora of molecular and genetic resources available for this organism have enabled us to test the significance of photoreceptor photocycle length of the VIVID (VVD) protein. Using defined in vitro mutations that alter the photocycle length of the VVD protein over 4 orders of magnitude we have been able dissect the functional ...
Sensing light from the environment using photoreceptors is of great adaptive significance to eukaryotes. A prominent feature of the photochemistry of these receptors is the photocycle length, the time taken to decay from the initial signaling light state back to the receptive dark state. Photoreceptors have distinct photocycle lengths and this suggests evolutionary selection of the photochemistry for biological function. However, the biological significance of the photocycle length is not understood as most in vivo studies with photoreceptors utilize true null or blind photoreceptor mutants. Neurospora crassa provides a fantastic template for studying photobiology and the plethora of molecular and genetic resources available for this organism have enabled us to test the significance of photoreceptor photocycle length of the VIVID (VVD) protein. Using defined in vitro mutations that alter the photocycle length of the VVD protein over 4 orders of magnitude we have been able dissect the functional ...
SzR was first identified in Asgardarchaeota and is phylogenetically positioned between typical microbial rhodopsins and HeRs (Fig. 1). In this study, we showed that SzR is a new type of light-driven inward H+ pump (Fig. 2). XeR was previously reported as an inward H+ pump in the typical microbial rhodopsin family (9-11). Although the sequential homology between the two subfamilies is low (SzR1 and PoXeR show 15.7% identity and 42.6% similarity), the trimeric structure and the photocycle with a large M accumulation not accompanied by N and O intermediates of SzR are similar to those reported for XeR (9-11), despite a large phylogenetic distance between them. This suggests that XeR and SzR underwent convergent evolution at the molecular level to achieve the same biological function. The differences and similarities between SzR and XeR are listed in Fig. 6C. Asgardarchaeota contain not only SzRs but also typical microbial rhodopsins with a DTK motif in helix C and HeRs (8). Although the function of ...
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 ...
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INTRODUCTION. In a recent report by Nishikawa et al. (1), the microorganisms isolated from the soil exhibited resistance towards benzalkonium chloride. Russel and co-workers have (2) proposed two possible mechanisms for such resistance: the intrinsic and acquired resistances. The intrinsic resistance related to the structural and chemical composition of the outer layers of the cells, which may provide an effective barrier to the entry of antibacterial agents. The acquired resistance results from genetic changes in the bacterial cell and arises either by mutation or by the acquisition of genetic material from another cell. Extensive investigations in the field of Schiff bases have been reported (3-5). Antimicrobial and antifungal activities of various Schiff bases ...
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