Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy

Maeda, Akio; Ohkita, Yoshihiro J.; Sasaki, Jun; Shichida, Yoshinori; Yoshizawa, Tôru

doi:10.1021/bi00096a013

Cited by 53 publications

(71 citation statements)

References 39 publications

(46 reference statements)

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“…The protonated state of Schiff base in octopus rhodopsin is probably stabilized by mechanisms other than direct charge neutralization. Polarization of and hydrogen bonding with nearby amino acid residues (including Tyr-112 and Asp-81) or water molecules are candidates for the stabilization mechanisms [36,37].…”

Section: Discussionmentioning

confidence: 99%

Ultraviolet resonance Raman evidence for the absence of tyrosinate in octopus rhodopsin and the participation of Trp residues in the transition to acid metarhodopsin

Hashimoto

Takeuchi

Nakagawa³

et al. 1996

FEBS Letters

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Section: Discussionmentioning

confidence: 99%

Ultraviolet resonance Raman evidence for the absence of tyrosinate in octopus rhodopsin and the participation of Trp residues in the transition to acid metarhodopsin

Hashimoto

Takeuchi

Nakagawa³

et al. 1996

FEBS Letters

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“…In some cases, assignment of vibrational bands to individual amino acid residues in rhodopsin was facilitated by site-directed mutagenesis (28,35). FTIR difference spectroscopy can also be used to study changes in the environment of individual water molecules in rhodopsin during the different steps in the photoactivation cascade (52)(53)(54). In this work, FTIR difference spectroscopy and amino acid isotope labeling were combined for the first time to analyze structural changes of tyrosines in rhodopsin.…”

Section: Figurementioning

confidence: 99%

Tyrosine Structural Changes Detected during the Photoactivation of Rhodopsin

DeLange¹,

Klaassen²,

Wallace-Williams³

et al. 1998

Journal of Biological Chemistry

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We present the first Fourier transform infrared (FTIR) analysis of an isotope-labeled eukaryotic membrane protein. A combination of isotope labeling and FTIR difference spectroscopy was used to investigate the possible involvement of tyrosines in the photoactivation of rhodopsin (Rho). Rho 3 MII difference spectra were obtained at 10°C for unlabeled recombinant Rho and isotope-labeled L-[ring-2 H 4 ]Tyr-Rho expressed in Spodoptera frugiperda cells grown on a stringent culture medium containing enriched L-[ring-2 H 4 ]Tyr and isolated using a His 6 tag. A comparison of these difference spectra revealed reproducible changes in bands that correspond to tyrosine and tyrosinate vibrational modes. A similar pattern of tyrosine/tyrosinate bands has also been observed in the bR 3 M transition in bacteriorhodopsin, although the sign of the bands is reversed. In bacteriorhodopsin, these bands were assigned to Tyr-185, which along with Pro-186 in the Fhelix, may form a hinge that facilitates ␣-helix movement.Elucidation of the mechanism of photoactivation of rhodopsin (Rho), 1 the light receptor in vision, remains an important problem in biology (1). Rhodopsin is an integral membrane protein found in the disc photoreceptor membranes of rod outer segments (2, 3) with a core structure consisting of seven transmembrane ␣-helices (4 -7). Upon light absorption, the rhodopsin chromophore, 11-cis-retinal, rapidly isomerizes to an alltrans configuration (8, 9) followed by a series of thermal transitions (Batho 3 Lumi 3 Meta I 3 Meta II) (10, 11). Signal transduction occurs upon formation of the Meta II intermediate, which binds and activates the G-protein transducin (12, 13). Because rhodopsin is a G-protein-coupled receptor, elucidation of its molecular mechanism is likely to be of general importance for the vast suprafamily of G-protein-coupled receptors, which include the ␤-adrenergic receptor (14, 15) and olfactory receptors (16).Thus far, bR is the only IMP with a seven-helix transmembrane motif whose structure has been elucidated at atomic resolution (17)(18)(19). This structure confirmed key features of an earlier "spectroscopic" model based in part on site-directed mutagenesis and FTIR difference spectroscopy (20 -23). For example, a retinal binding pocket was predicted on the basis of FTIR, UV-visible spectroscopy, and site-directed mutagenesis (20 -24), which is formed in part from several residues on the F-helix (helix 6 in rhodopsin), including two tryptophans (Trp-182, Trp-189), a proline (Pro-186), and a tyrosine (Tyr-185). These residues, along with several others from the C-helix (Trp-86, Thr-89, and Asp-85) are in close proximity to the retinal chromophore and act to constrain its structure in an all-trans configuration. In addition, these residues are in a good position to couple retinal isomerization to protein changes involved in proton transport, including a change in the structure and orientation of the F-helix.A comparable combination of Trp, Pro, and Tyr residues (WXPY) is fully conserved in helix 6 of all ...

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“…4 The structural dynamics of rhodopsin activation and the structural basis of its unique physiological functions are determined, to a large extent, by dynamic H-bonded networks and ionic interactions. [5][6][7][8][9] Much of our knowledge regarding these networks and interactions has been obtained using spectroscopic techniques, and in particular infrared vibrational spectroscopy, often in combination with site-directed mutagenesis, [10][11][12][13][14][15][16] or NMR spectroscopy. 17,18 Rhodopsin activation is initiated by photoisomerization of its 11-cis retinylidene chromophore, which is linked to the protein by a protonated Schiff base (PSB), to an all-trans geometry.…”

Section: Introductionmentioning

confidence: 99%