Carotenoid response to retinal excitation and photoisomerization dynamics in xanthorhodopsin

Šlouf, Václav; Balashov, Sergei P.; Lanyi, Janos Κ.; Pullerits, Tõnu; Polı́vka, Tomáš

doi:10.1016/j.cplett.2011.09.062

Cited by 12 publications

(17 citation statements)

References 31 publications

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“…The formation of intermediate K 590 , which has a microsecond lifetime, completes the process of converting the energy of a light quantum into chemical energy in the form of conformational changes in the protein, which are subsequently used for proton transfer. In bR, an additional excited state decay in the picosecond timescale with a low amplitude was observed, which does not lead to retinal isomerization. ,,,,,,, …”

Section: Introductionmentioning

confidence: 91%

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Comparative Femtosecond Spectroscopy of Primary Photoreactions of Exiguobacterium sibiricum Rhodopsin and Halobacterium salinarum Bacteriorhodopsin

et al. 2021

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The primary stages of the Exiguobacterium sibiricum rhodopsin (ESR) photocycle were investigated by femtosecond absorption laser spectroscopy in the spectral range of 400−900 nm with a time resolution of 25 fs. The dynamics of the ESR photoreaction were compared with the reactions of bacteriorhodopsin (bR) in purple membranes (bR PM ) and in recombinant form (bR rec ). The primary intermediates of the ESR photocycle were similar to intermediates I, J, and K in bacteriorhodopsin photoconversion. The CONTIN program was applied to analyze the characteristic times of the observed processes and to clarify the reaction scheme. A similar photoreaction pattern was observed for all studied retinal proteins, including two consecutive dynamic Stokes shift phases lasting ∼0.05 and ∼0.15 ps. The excited state decays through a femtosecond reactive pathway, leading to retinal isomerization and formation of product J, and a picosecond nonreactive pathway that leads only to the initial state. Retinal photoisomerization in ESR takes 0.69 ps, compared with 0.48 ps in bR PM and 0.74 ps in bR rec . The nonreactive excited state decay takes 5 ps in ESR and ∼3 ps in bR. We discuss the similarity of the primary reactions of ESR and other retinal proteins.

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Section: Introductionmentioning

confidence: 91%

“…The photochemistry of a number of microbial proton pumps ,,,− and some of their mutants ,, has been studied intensely. The primary reactions occurring in the femto- and picosecond time ranges share much in common.…”

Section: Introductionmentioning

confidence: 99%

Comparative Femtosecond Spectroscopy of Primary Photoreactions of Exiguobacterium sibiricum Rhodopsin and Halobacterium salinarum Bacteriorhodopsin

et al. 2021

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“…Salinixanthin is found in close proximity to the retinal, acting as an antenna pigment to collect light for proton pumping by xanthorhodopsin. The antenna carotenoid extends the wavelength range of light collection for transmembrane proton transport (Balashov et al ., , ; Boichenko et al ., ; Balashov & Lanyi, ; Šlouf et al ., ). Light energy absorbed by the carotenoid is transferred to the retinal with a quantum efficiency of ~40–45% (Polívka et al ., ).…”

Section: Pigments and Their Functionsmentioning

confidence: 97%

Salinibacter: an extremely halophilic bacterium with archaeal properties

Oren

2013

FEMS Microbiol Lett

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The existence of large number of a member of the Bacteroidetes in NaCl-saturated brines in saltern crystallizer ponds was first documented in 1999 based on fluorescence in situ hybridization studies. Isolation of the organism and its description as Salinibacter ruber followed soon. It is a rod-shaped, red-orange pigmented, extreme halophile that grows optimally at 20-30% salt. The genus is distributed worldwide in hypersaline environments. Today, the genus Salinibacter includes three species, and a somewhat less halophilic relative, Salisaeta longa, has also been documented. Although belonging to the Bacteria, Salinibacter shares many features with the Archaea of the family Halobacteriaceae that live in the same habitat. Both groups use KCl for osmotic adjustment of their cytoplasm, both mainly possess salt-requiring enzymes with a large excess of acidic amino acids, and both contain different retinal pigments: light-driven proton pumps, chloride pumps, and light sensors. Salinibacter produces an unusual carotenoid, salinixanthin that forms a light antenna and transfers energy to the retinal group of xanthorhodopsin, a light-driven proton pump. Other unusual features of Salinibacter and Salisaeta include the presence of novel sulfonolipids (halocapnine derivatives). Salinibacter has become an excellent model for metagenomic, biogeographic, ecological, and evolutionary studies.

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“…Studying the new rep resentatives of the family supplements our knowledge of the structural basis of such transport [66] and promotes their application in bio optoelectronics as a basis for molecular memory elements and photoactive media in dynamic holography [70 72], and in a new field -opto genetics [73] -for regulation of neuronal activity [74 76]. The sensitivity of photocycle reaction kinetics and fluorescence of the proton pumps to electrochemical potentials [77,78] revealed the possibility of using them as sensors for detection of intraprotein [79] and trans membrane changes of potentials [80].…”

Section: Extracellular Mediummentioning

confidence: 99%

ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

Petrovskaya

Balashov

Лукашев

et al. 2015

Biochemistry Moscow

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This review covers the properties of a retinal protein (ESR) from the psychrotrophic bacterium Exiguobacterium sibiricum that functions as a light-driven proton pump. The presence of a lysine residue at the position corresponding to intramolecular proton donor for the Schiff base represents a unique structural feature of ESR. We have shown that Lys96 successfully facilitates delivery of protons from the cytoplasmic surface to the Schiff base, thus acting as a proton donor in ESR. Since proton uptake during the photocycle precedes Schiff base reprotonation, we conclude that this residue is initially in the uncharged state and acquires a proton for a short time after Schiff base deprotonation and M intermediate formation. Involvement of Lys as a proton donor distinguishes ESR from the related retinal proteins - bacteriorhodopsin (BR), proteorhodopsin (PR), and xanthorhodopsin (XR), in which the donor function is performed by residues with a carboxyl side chain. Like other eubacterial proton pumps (PR and XR), ESR contains a histidine residue interacting with the proton acceptor Asp85. In contrast to PR, this interaction leads to shift of the acceptor's pKa to more acidic pH, thus providing its ability to function over a wide pH range. The presence of a strong H-bond between Asp85 and His57, the structure of the proton-conducting pathways from cytoplasmic surface to the Schiff base and to extracellular surface, and other properties of ESR were demonstrated by solving its three-dimensional structure, which revealed several differences from known structures of BR and XR. The structure of ESR, its photocycle, and proton transfer reactions are discussed in comparison with homologous retinal proteins.

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Carotenoid response to retinal excitation and photoisomerization dynamics in xanthorhodopsin

Cited by 12 publications

References 31 publications

Comparative Femtosecond Spectroscopy of Primary Photoreactions of Exiguobacterium sibiricum Rhodopsin and Halobacterium salinarum Bacteriorhodopsin

Comparative Femtosecond Spectroscopy of Primary Photoreactions of Exiguobacterium sibiricum Rhodopsin and Halobacterium salinarum Bacteriorhodopsin

Salinibacter: an extremely halophilic bacterium with archaeal properties

ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum

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