Photolysis intermediates of the artificial visual pigment cis-5,6-dihydro-isorhodopsin

Albeck, A.; Friedman, Noga; Ottolenghi, Michael; Sheves, Mordechai; Einterz, C. M.; Hug, Stephan J.; Lewis, James W.; Kliger, David S.

doi:10.1016/s0006-3495(89)82798-5

Cited by 46 publications

(50 citation statements)

References 30 publications

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“…These retinal analogues cause an altered photoreaction (Albeck et al 1989;Shichida et al 1981;Ganter et al 1989). In 9-H-rhodopsin, transducin is activated to only a very limited extent .…”

Section: Introductionmentioning

confidence: 99%

The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy

1990

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The photoreaction of rhodopsin regenerated with l l-cis-13-demethyl-retinal was investigated by FTIR difference spectroscopy. The measurements show that the chromophore experiences different twists in the modified bathorhodopsin as compared to normal bathorhodopsin and that the twists are relaxed .in the additional intermediate batho-lumirhodopsin. Whereas the missing methyl group influences the lumimetarhodopsin-I transition, a metarhodopsin-I-metarhodopsin-II difference spectrum very similar to that of unmodified rhodopsin is observed. The significance of the steric interaction for regulating the photoreaction is discussed.

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“…These retinal analogues cause an altered photoreaction (Albeck et al 1989;Shichida et al 1981;Ganter et al 1989). In 9-H-rhodopsin, transducin is activated to only a very limited extent .…”

Section: Introductionmentioning

confidence: 99%

The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy

1990

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“…The photobleaching process of rhodopsin has been investigated using retinal analogs that contained an extra ring between C 10 and C 13 , making retinal non-isomerizable around the 11-cis double bond (7)(8)(9)(10)(11)(12)). An artificial visual pigment with restricted C 9 -C 11 motion forms normal photolysis intermediates (13), suggesting an importance of C 11 ϭC 12 bond isomerization in the activation of Rho.…”

mentioning

confidence: 99%

“…An artificial visual pigment with restricted C 9 -C 11 motion forms normal photolysis intermediates (13), suggesting an importance of C 11 ϭC 12 bond isomerization in the activation of Rho. More recently, it was reported that after photoisomerization, the ␤-ionone ring of the chromophore moves to a new position during the transition to Meta II (7).…”

mentioning

confidence: 99%

Biochemical and Physiological Properties of Rhodopsin Regenerated with 11-cis-6-Ring- and 7-Ring-retinals

Kuksa¹,

Bartl

Maeda³

et al. 2002

Journal of Biological Chemistry

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Phototransduction is initiated by the photoisomerization of rhodopsin (Rho) chromophore 11-cis-retinylidene to all-trans-retinylidene. Here, using Rho regenerated with retinal analogs with different ring sizes, which prevent isomerization around the C 11 ‫؍‬C 12 double bond, the activation mechanism of this G-protein-coupled receptor was investigated. We demonstrate that 11-cis-7-ring-Rho does not activate G-protein in vivo and in vitro, and that it does not isomerize along other double bonds, suggesting that it fits tightly into the binding site of opsin. In contrast, bleaching 11-cis-6-ring-Rho modestly activates phototransduction in vivo and at low pH in vitro. These results reveal that partial activation is caused by isomerization along other double bonds in more rigid 6-locked retinal isomers and protonation of key residues by lowering pH in 11-cis-6-ring-Rhos. Full activation is not achieved, because isomerization does not induce a complete set of conformational rearrangements of Rho. These results with 6-and 7-ringconstrained retinoids provide new insights into Rho activation and suggest a potential use of locked retinals, particularly 11-cis-7-ring-retinal, to inactivate opsin in some retinal degeneration diseases.In vertebrate retinal photoreceptor cells, isomerization of the visual pigment chromophore, 11-cis-retinal to all-trans-retinal, triggers a set of reactions collectively termed the phototransduction cascade (1, 2). The phototransduction events are initiated by activated rhodopsin (Rho*) 1 and progress through a classical G-protein cascade, ultimately leading to neuronal signaling. Metarhodopsin II (or Meta II, Rho*), the catalytically active intermediate generated by photoisomerization of Rho chromophore, contains all-trans-retinal covalently bound to Lys 296 of opsin via the deprotonated Schiff base. Subsequently, Meta II undergoes reprotonation, and the photolyzed chromophore is hydrolyzed and released from opsin (3-5). The precise mechanism of Rho activation by the photoisomerized chromophore is unknown (6).The photobleaching process of rhodopsin has been investigated using retinal analogs that contained an extra ring between C 10 and C 13 , making retinal non-isomerizable around the 11-cis double bond (7-12). An artificial visual pigment with restricted C 9 -C 11 motion forms normal photolysis intermediates (13), suggesting an importance of C 11 ϭC 12 bond isomerization in the activation of Rho. More recently, it was reported that after photoisomerization, the ␤-ionone ring of the chromophore moves to a new position during the transition to Meta II (7). Jang et al. (14) showed using 6-ring-constrained retinal isomers and the crystal structure of Rho in the ground state (15) that if this movement is restricted, only residual activity could be observed. Locked retinal analogs were also used to study visual transduction in vivo using vitamin A-deprived rats (16, 17). These animals had approximately half of the normal complement of rhodopsin, and injection of locked retinal led to the appearan...

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“…On a nanosecond time scale, Batho is in equilibrium with the blue-shifted intermediate (BSI), which decays to form lumirhodopsin (Lumi), an intermediate with a lifetime of microseconds. [13][14][15][16] The dynamic details of the process has been well-studied by previous molecular dynamics simulations. 36,38,49 In this work, we evaluated the contributions of each residues in terms of EAWs during the transition from Batho to BSI, which is the preliminary step towards a thorough understanding of the whole photo-activation process and also of profound implications for protein-ligand interactions.…”

mentioning

confidence: 99%

Residue-Residue Mutual Work Analysis of Retinal-Opsin Interaction in Rhodopsin: Implications for Protein-Ligand Binding

2019

Preprint

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Energetic contributions at single-residue level to retinal-opsin interaction in rhodopsin were studied by combining molecular dynamics simulations, transition path sampling, and a newly developed energy decomposition approach. The virtual work at an infinitesimal time interval was decomposed into the work components on one residue due to its interaction with another residue, which were then averaged over the transition path ensemble along a proposed reaction coordinate. Such residueresidue mutual work analysis on 62 residues within the active center of rhodopsin resulted in a very sparse interaction matrix, which is generally not symmetric but anti-symmetric to some extent. 14 residues were identified to be major players in retinal relaxation, which is in excellent agreement with an existing NMR study. Based on the matrix of mutual work, a comprehensive network was constructed to provide detailed insights into the chromophore-protein interaction from a viewpoint of energy flow.

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Photolysis intermediates of the artificial visual pigment cis-5,6-dihydro-isorhodopsin

Cited by 46 publications

References 30 publications

The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy

The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy

Biochemical and Physiological Properties of Rhodopsin Regenerated with 11-cis-6-Ring- and 7-Ring-retinals

Residue-Residue Mutual Work Analysis of Retinal-Opsin Interaction in Rhodopsin: Implications for Protein-Ligand Binding

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