An FTIR Study of Monkey Green‐ and Red‐Sensitive Visual Pigments

Katayama, Kota; Furutani, Yuji; Imai, Hiroo; Kandori, Hideki

doi:10.1002/ange.200903837

Cited by 12 publications

(42 citation statements)

References 33 publications

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“… 140 This trend seems to be general for animal rhodopsins, since similarly enhanced HOOP modes were observed for squid rhodopsin 144 and color visual pigments. 145 Relaxation of the distorted polyene chain leads to the formation of lumirhodopsin, signifying energy transfer to the opsin moiety, as was clearly observed by X-ray crystallography. 146 The bathointermediate is ∼150 kJ/mol higher in energy than the dark state of rhodopsin, and activation energy for the isomerization (Figure 7 ) is estimated to be larger than 180 kJ/mol.…”

Section: Light Absorption and Photoisomerizationmentioning

confidence: 82%

Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

et al. 2013

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Section: Light Absorption and Photoisomerizationmentioning

confidence: 82%

Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

et al. 2013

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“…To gain insight into the molecular mechanism of photoactivation, it is necessary to purify and characterize the full-length protein. Although expression levels of rhodopsins are usually much smaller in HEK293T cells than in yeast and Escherichia coli, previously, we have been able to conduct infrared spectroscopic studies on monkey red-and green-sensitive pigments based on HEK293 cell expression (31,32). We thus applied the sample preparation procedure as used for monkey red-and green-sensitive pigments to Rh-PDE, using HEK293T cell expression, solubilization by dodecyl-␤-D-maltopyranoside (DDM), and purifica-tion by monoclonal antibody column chromatography, with all-trans-retinal being added into the culture medium.…”

Section: Molecular Properties Of Purified Full-length Rh-pdementioning

confidence: 99%

A unique choanoflagellate enzyme rhodopsin exhibits light-dependent cyclic nucleotide phosphodiesterase activity

Yoshida¹,

Tsunoda

Brown

et al. 2017

Journal of Biological Chemistry

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Photoactivated adenylyl cyclase (PAC) and guanylyl cyclase rhodopsin increase the concentrations of intracellular cyclic nucleotides upon illumination, serving as promising second-generation tools in optogenetics. To broaden the arsenal of such tools, it is desirable to have light-activatable enzymes that can decrease cyclic nucleotide concentrations in cells. Here, we report on an unusual microbial rhodopsin that may be able to meet the demand. It is found in the choanoflagellate and contains a C-terminal cyclic nucleotide phosphodiesterase (PDE) domain. We examined the enzymatic activity of the protein (named Rh-PDE) both in HEK293 membranes and whole cells. Although Rh-PDE was constitutively active in the dark, illumination increased its hydrolytic activity 1.4-fold toward cGMP and 1.6-fold toward cAMP, as measured in isolated crude membranes. Purified full-length Rh-PDE displayed maximal light absorption at 492 nm and formed the M intermediate with the deprotonated Schiff base upon illumination. The M state decayed to the parent spectral state in 7 s, producing long-lasting activation of the enzyme domain with increased activity. We discuss a possible mechanism of the Rh-PDE activation by light. Furthermore, Rh-PDE decreased cAMP concentration in HEK293 cells in a light-dependent manner and could do so repeatedly without losing activity. Thus, Rh-PDE may hold promise as a potential optogenetic tool for light control of intracellular cyclic nucleotides ( to study cyclic nucleotide-associated signal transduction cascades).

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“…11 Between RH1 and M/LWS opsins, there are four identical AA changes in helix III (sites A117V, T118S, G120C, E122I); one in helix IV at site A164S in red-opsin; three in the E-II loop at sites E181H, I189P, Y191V; four in helix V at sites M207L, F208M, H211C, F212C; two at sites F261Y, A269T in red-opsin; and one in helix VII at site F293Y. 12 …”

Section: Computationalmentioning

confidence: 99%

“…The residue numbers are based on the bovine rhodopsin sequence. This figure is taken from reference 12.…”

Section: Figurementioning

confidence: 99%

Color Vision: “OH-Site” Rule for Seeing Red and Green

et al. 2012

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Eyes gather information and color forms an extremely important component of the information, more so in the case of animals to forage and navigate within their immediate environment. By using the ONIOM (QM/MM) method, we report a comprehensive theoretical analysis of the structure and molecular mechanism of spectral tuning of monkey-red and green-sensitive visual pigments. We show that, interaction of retinal with three hydroxyl-bearing amino acids near the β-ionone ring part of the retinal in opsin, A164S, F261Y and A269T, increases the electron delocalization, decreases the BLA of the retinal and leads to variation in the wavelength of maximal absorbance in the red- and green-sensitive visual pigments. Based on the analysis, we propose the “OH-site” rule for seeing red and green. This rule is also shown to account for the spectral shifts obtained from hydroxyl-bearing amino acids near the Schiff base in different visual pigments: at site 292 (A292S, A292Y, and A292T) in bovine and at site 111 (Y111) in squid opsins. Therefore, the OH-site rule is shown to be site-specific and not pigment-specific and thus can be used for tracking spectral shifts in any visual pigment.

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An FTIR Study of Monkey Green‐ and Red‐Sensitive Visual Pigments

Cited by 12 publications

References 33 publications

Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

A unique choanoflagellate enzyme rhodopsin exhibits light-dependent cyclic nucleotide phosphodiesterase activity

Color Vision: “OH-Site” Rule for Seeing Red and Green

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