Light-induced protein conformational changes in the photolysis of octopus rhodopsin

Nakagawa, Masashi; Kikkawa, Shōichi; Iwasa, Takeshi; Tsuda, Motoyuki

doi:10.1016/s0006-3495(97)78876-3

Cited by 13 publications

(18 citation statements)

References 27 publications

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“…Transient transmittance changes were measured using a modified version of a laser photolysis apparatus that had been described previously [4]. When the chromophore absorption changes were measured at 530 nm over a long time range, the probe light was reduced by a neutral density filter to minimize the photolysis by the probe beam.…”

Section: Methodsmentioning

confidence: 99%

“…Rhodopsin is a system par excellence to study the molecular mechanisms of the activation of a G‐protein by its receptor [1–3]. Upon absorbing a photon, the retinal chromophore isomerizes from 11‐ cis to all‐ trans which leads to protein conformational changes of the pigment [4]. Although vertebrate rhodopsin has several photointermediates, most evidence has suggested that a particular intermediate, metarhodopsin II, is the one that can activate transducin in vertebrate photoreceptors.…”

Section: Introductionmentioning

confidence: 99%

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A novel photointermediate of octopus rhodopsin activates its G‐protein

et al. 1998

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The photointermediate of octopus rhodopsin responsible for G-protein activation was examined by a GTPQ QS-binding assay in a reconstituted system with purified rhodopsin and photoreceptor G-protein. When octopus rhodopsin alone was incubated in the dark after illumination, its ability to stimulate GTPQ QS-binding by the G-protein decreased in a time-dependent manner. We associate this decay with the decay of a novel photointermediate, transient acid metarhodopsin, which lies between mesorhodopsin and acid metarhodopsin. Spectroscopic evidence for its existence was suggested by its effects on the turbidity of the vesicles. These results suggest that the transient acid metarhodopsin, not the stable final photoproduct, acid metarhodopsin, activates a G-protein in octopus photoreceptors.z 1998 Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A novel photointermediate of octopus rhodopsin activates its G‐protein

et al. 1998

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“…The addition of the neutral surfactants C6E2 and C6E1 to the bR solution did not cause a significant change in absorption maximum and absorbance. As seen in inset (i), The change in the absorbance for the aromatic protein residues reflects changes in the local chemical environment (50). Given the lack of spectral overlap between the surfactants and bR around 280 nm, the ratio of A 280 nm ⁄ A 568 nm can be used to indicate the extent of denaturation of bR upon surfactant treatment.…”

Section: Steady-state Uv-vis Spectral Behavior Of Pm Suspension In Thmentioning

confidence: 99%

Kinetics of the M‐Intermediate in the Photocycle of Bacteriorhodopsin upon Chemical Modification with Surfactants

Chu

El‐Sayed

2010

Photochem & Photobiology

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The spectroscopic and kinetic studies of the interaction between bacteriorhodopsin in the M-intermediate and several surfactants (cetyl trimethyl ammonium bromide, dodecyl trimethyl ammonium bromide, diethylene glycol mono-n-hexyl ether, ethylene glycol mono-n-hexyl ether, sodium 1-decanesulfonate and sodium 1-heptanesulfonate) have been investigated using steady-state UV-VIS spectrometry and time-resolved absorption techniques. The steady-state spectral results show that bR retains its trimeric state. Time-resolved observations indicate that the rate of deprotonation of the protonated Schiff base increases in the presence of the cationic surfactants, whereas insignificant changes are observed in the neutral or anionic surfactants. The rate of the reprotonation of the Schiff base in the transition M --> N is accelerated in anionic and neutral surfactants, but is decelerated in the presence of the cationic surfactants. Surfactants with a longer hydrocarbon tail have a greater effect on the kinetics when compared with surfactants having shorter hydrocarbon tails. The opposite effect is observed when the hydrophilic head of the surfactants contains opposite charges. These distinct kinetics are discussed in terms of the difference in the modified surface hydrophilicity of the bR and the possible protein configurational changes upon surfactant treatments.

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“…The concentration of OR is 3.15 mg/mL, and pure grade of each sample was performed 19 taking into consideration the absorbance values at A 280 and absorbance maximum at A 482 , and was estimated as 18.6%.…”

Section: Spectral Determination and Other Analytical Methodsmentioning

confidence: 99%

Photoreversibility and photostability in films of octopus rhodopsin isolated from octopus photoreceptor membranes

Paternolli¹,

Neebe²,

Stura³

et al. 2008

J Biomedical Materials Res

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In this work, a new biomaterial resulting from the isolation of octopus rhodopsin (OR) starting from octopus photoreceptor membranes is presented. Mass spectroscopic characterization was employed in order to verify the presence of rhodopsin in the extract. Photoreversibility and photochromic properties were investigated using spectrophotometric measurements and pulsed light. Thin films of OR were realized using the gel-matrix entrapment method in polyvinyl alcohol solution. The results indicate that the photoreversibility and the photostability of the OR in gel-matrices are maintained. Several measurements were performed to test the stability of the resulting biomaterial in time and at room temperature. Preliminary tests demonstrate that the photoreversibility and the photostability are still found after few days from the biomaterial preparation and after the exposure for several hours at room temperature.

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Light-induced protein conformational changes in the photolysis of octopus rhodopsin

Cited by 13 publications

References 27 publications

A novel photointermediate of octopus rhodopsin activates its G‐protein

A novel photointermediate of octopus rhodopsin activates its G‐protein

Kinetics of the M‐Intermediate in the Photocycle of Bacteriorhodopsin upon Chemical Modification with Surfactants

Photoreversibility and photostability in films of octopus rhodopsin isolated from octopus photoreceptor membranes

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