Rhodopsins containing 6- to 9-membered rings. The triggering process of visual transduction

Nakanishi, Koji; Chen, Arh‐Hwang; Derguini, Fadila; Franklin, Paul J.; Hu, Shuanghua; Wang, Jun

doi:10.1351/pac199466050981

Cited by 10 publications

(4 citation statements)

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“…Studies on Rh RT regenerated with structurally modified retinals that are selected to remove steric constraints produce different photoreactions and can diminish/abolish G-protein activation . Other studies of Rh regenerated with structurally modified retinals have investigated reaction rates, quantum yields, the isomerization mechanism, and retinal/protein interactions. ,, …”

Section: Discussionmentioning

confidence: 99%

“…56 Other studies of Rh regenerated with structurally modified retinals have investigated reaction rates, quantum yields, the isomerization mechanism, and retinal/protein interactions. 31,57,58 All of these data suggest that the retinal is located within a small, spatially constrained protein binding pocket. Upon the 11-cis to all-trans isomerization within retinal, new retinalprotein interactions lead to new spatial constraints and steric interactions between the retinal and the protein that must be…”

Section: Energy Storage/transduction Mechanism (A) Cdc Stretching Fre...mentioning

confidence: 94%

“…FTIR data provide evidence that Glu-113 is the counterion in the Rh RT photoreaction, , while NMR results have located the counterion within the protein adjoining the retinal Rh RT , and batho LT . , Transient ultraviolet and visible absorption spectroscopy on Rh RT samples containing both native and modified retinals have identified the intermediates comprising the Rh RT photoreactions. ,,, Time-resolved fluorescence studies have determined the excited-state lifetime of Rh RT , and of the 11- cis chromophore in solution …”

Section: A Introductionmentioning

confidence: 99%

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Vibrational Spectrum of Bathorhodopsin in the Room-Temperature Rhodopsin Photoreaction

1997

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Picosecond time-resolved coherent anti-Stokes Raman spectroscopy (PTR/CARS) is used to generate high signal to noise (S/N) vibrational spectra of bathorhodopsin (batho) formed in the photoreaction of room-temperature rhodopsin (RhRT). These PTR/CARS spectra of bathoRT, measured as a function of only the time following 3-ps (full width at half maximum), 500-nm excitation of RhRT, demonstrate that the vibrational structure of bathoRT in the 700−1700-cm-1 region is distinct from that of RhRT and remains unchanged over at least the 10 ps [8 ps cross correlation time (CCT)] to 100 ns interval of the RhRT photoreaction. Given the experimental difficulties associated with the irreversibility of the RhRT photoreaction, these are the first time-resolved vibrational spectra of bathoRT over the full 700−1700-cm-1 region to be reported. The PTR/CARS spectra taken after 100 ns contain vibrational features other than those assignable to either RhRT or bathoRT (potentially assignable to the blue-shifted intermediate, BSI). Excellent agreement is found between the major features of the RhRT and bathoRT vibrational spectra measured via PTR/CARS and earlier resonance Raman (RR) spectra taken at low temperatures (LT) selected to thermally stabilize (freeze) batho. Comparisons of the CC stretching mode region reveal a 12-cm-1 shift upon bathoRT formation (PTR/CARS data), which agrees well with the 13-cm-1 shift found for batho trapped at LT (RR data). These vibrational frequency changes also correlate well with the corresponding 38-nm (LT) and 31-nm (RT) shifts observed in the absorption maxima upon the formation of batho, thereby supporting an inverse relationship between CC frequencies and absorption maxima proposed for retinal proteins. Comparisons of the CC stretching frequencies at LT and RT reveal a temperature dependence characterized by red shifts of 4 cm-1 in Rh and 3 cm-1 in batho, the direction of which is opposite to the blue shifts observed in the visible absorption maxima of Rh (7 nm) and batho (14 nm). This latter observation suggests a stronger interaction of the protein (likely with the counterion Glu-113) with the all-trans-retinal in the bathoRT structure than in the corresponding static bathoLT structure.

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Section: Discussionmentioning

confidence: 99%

Section: Energy Storage/transduction Mechanism (A) Cdc Stretching Fre...mentioning

confidence: 94%

Section: A Introductionmentioning

confidence: 99%

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Vibrational Spectrum of Bathorhodopsin in the Room-Temperature Rhodopsin Photoreaction

1997

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“…The protein continues its thermal relaxation to give further intermediates, 7 leading eventually to the all-trans-retinal and the apoprotein opsin. 8 Since the originally orange-colored Rh becomes nearly colorless at this stage, the whole process is called bleaching. The alltrans-retinal is then reduced to retinol ͑vitamin A͒, esterified, isomerized to 11-cis-retinol, which is oxidized to 11-cisretinal, and recombines with opsin to produce Rh.…”

Section: Introductionmentioning

confidence: 99%

Ab initiostudy on the low-lying excited states of retinal

Merchán

González‐Luque

1997

The Journal of Chemical Physics

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Ab initio results for the electronic spectrum of all-trans-retinal and its truncated model 3-methyl-all-trans (10-s-cis)-2,4,6,8,10-undecapentaen-1-al are presented. The study includes geometry determination of the ground state. Vertical excitation energies have been computed using multiconfigurational second-order perturbation theory through the CASPT2 formalism. The lowest singlet excited state in gas phase is predicted to be of nπ* character. The lowest triplet state corresponds, however, to a ππ* state. The most intense feature of the spectrum is due to the strongly dipole-allowed ππ* transition, in accordance with the observed maximum in the one-photon spectra. The vertical excitation energies of the Bu- and Ag-like states are found close, the latter ≈1 eV higher than the maximum in the two-photon spectra. Solvent effects and nonvertical nature of the observed maximum in the two-photon spectra are invoked in rationalizing the deviation with respect to the best present estimate for the Ag-like state. In addition, qualitative aspects of the one-bond photoisomerization about the C11=C12 double bond of retinal are considered. The overall isomerization picture from 11-cis into all-trans-retinal, as taking place mainly along the triplet manifold, agrees with experimental evidence.

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ChemInform Abstract: Rhodopsins Containing 6‐ to 9‐Membered Rings. The Triggering Process of Visual Transduction.

et al. 1994

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Rhodopsins containing 6- to 9-membered rings. The triggering process of visual transduction

Abstract: Abstract

Cited by 10 publications

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Vibrational Spectrum of Bathorhodopsin in the Room-Temperature Rhodopsin Photoreaction

Vibrational Spectrum of Bathorhodopsin in the Room-Temperature Rhodopsin Photoreaction

Ab initiostudy on the low-lying excited states of retinal

ChemInform Abstract: Rhodopsins Containing 6‐ to 9‐Membered Rings. The Triggering Process of Visual Transduction.

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