Vibrational analysis of 13-cis-retinal

Curry, Bo; Palings, I.; Broek, Albert; Pardoen, J. A.; Mulder, Patrick P.J.; Lugtenburg, J.; Mathies, Richard A.

doi:10.1021/j150648a015

Cited by 71 publications

(114 citation statements)

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“…However, the spectral feature of the C 14 -HOOP band at 864 cm -1 is consistent with that of the C 14 -D stretching band at 2244 cm -1 . It should be noted that the C 14 -HOOP mode is located at a frequency 33 cm -1 higher than that of the 13-cis-retinal (831 cm -1 ) (22) and is closer to that of the all-trans-retinal (876 cm -1 ) (23). This indicates that the chromophore of SRII K is in an unrelaxed 13-cis configuration.…”

Section: Hydrogen Out-of-plane (Hoop) Vibrations Of the Retinal In Srmentioning

confidence: 97%

Steric Constraint in the Primary Photoproduct of an Archaeal Rhodopsin from Regiospecific Perturbation of C−D Stretching Vibration of the Retinyl Chromophore

et al. 2005

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In visual and archaeal rhodopsins, light energy is stored in the chromophore−protein interaction after retinal photoisomerization. This paper reports a novel method to monitor the steric constraint after retinal isomerization by use of enhanced C−D stretching vibrations. In the difference FTIR spectra between an archaeal light-sensor pharaonis phoborhodopsin (ppR) and the primary K intermediate at 77 K, no peaks were observed in the 2160−2330 cm-1 region for deuterated retinals at position 7, 8, 10, 11, 12, and 15, whereas a strong peak appeared at 2244 cm-1 for the K intermediate of ppR possessing a C14−D-labeled retinal. The 2244-cm-1 band is assigned as the C14−D stretching vibration, and enhanced absorption in the K state probably originates from the local steric constraint at the C14−D position (also possible electrostatic field effects) after the C13C14 double bond rotation.

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Section: Hydrogen Out-of-plane (Hoop) Vibrations Of the Retinal In Srmentioning

confidence: 97%

Steric Constraint in the Primary Photoproduct of an Archaeal Rhodopsin from Regiospecific Perturbation of C−D Stretching Vibration of the Retinyl Chromophore

et al. 2005

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“…The use of 13C-labelled retinals has been essential to effect the complete vibrational analysis of all-trans -l3cis, I Icis, 9cis and 9 I3dicis retinal (Ref. 31). The complete vibrational analysis of the chromophores in bacteriorhodopsin, rhodopsin and their photoproducts are in progress.…”

Section: Synthesis Of 13c-lahelled Retinalsmentioning

confidence: 99%

The synthesis of 13C-labelled retinals

Lugtenburg¹

1985

Pure and Applied Chemistry

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“…Substantial progress has been made in understanding the vibrational nor- ma1 modes of these molecules, particularly those of retinal isomers (cf. Curry et al, 1985). It is convenient and meaningful to group these observed bands into a number of separate regions that reflect the nature of the normal modes.…”

Section: Resultsmentioning

confidence: 99%

“…The spectral pattern is quite different for the all-trans, 13-cis, 11-cis, and 9 4 s retinal isomers (cf. Curry et al, 1985). All peak positions and intensity ratios of retinal in CC1, in the fingerprint region (Fig.…”

Section: Fingerprint Regionmentioning

confidence: 99%

The interactions of retinoids with retinol‐binding protein

Manor

Callender

Noy

1993

European Journal of Biochemistry

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We have measured the pre-resonance Raman spectrum of retinal, retinoic acid and retinol in dilute CCl, solutions and when bound to the bovine-serum retinol-binding protein. The comparison reveals that the binding interaction does not involve any specific interactions of the head group and/ or the polyene chain with a particular protein residue. The data indicate hydrogen bonding of bound retinal's head-group oxygen to water, as well as some torsional angle change of its polyene chain upon binding.Retinol (vitamin A alcohol) circulates in blood bound to retinol-binding protein (RBP), a single polypeptide with a molecular mass of 21 kDa that has a single binding site for retinoids (Goodman, 1984). In the circulation, holo-RBP is complexed with another plasma protein, transthyretin. The three-dimensional structure of holo-RBP was determined by X-ray crystallography, and shows that it is composed of a single globular domain comprised of an N-terminal coil, a asheet core, an a-helix, and a C-terminal coil (Cowan et al., 1990;Newcomer et al., 1984). The core of RBP is composed of eight antiparallel p strands which are arranged in two stacked orthogonal p sheets. Retinol is encapsulated within the j? sheets with the p-ionone ring positioned deep within the /? barrel and the isoprene tail extending along the barrel axis to near the surface of the protein.The selectivity of RBP for binding various retinoids and other hydrophobic compounds has been hard to decipher from competition experiments despite intensive efforts. While some groups reported similar affinity of RBP for retinol, citral and p-ionone (Hase et al., 1976), and interpreted the results to indicate lack of a requirement for a fixed polyene chain length, others (Honvitz and Heller, 1974) reported no binding of p-ionone, deducing the opposite conclusion. The isomeric conformation of retinoids was reported to have no effect on binding in some cases (Horwitz and Heller, 1973) and to completely inhibit binding in others (Siegenthaler and Saurat, 1987). Similarly, conflicting reports were published regarding the necessity of a six-membered ring structure as well as a specific requirement of the polar group on the isoprene tail (Goodman and Raz, 1972;Hase et al., 1976; Honvitz and Heller, 1974 recent study of the thermodynamic parameters that contribute to the binding of retinol to RBP have shown that binding is stabilized purely by an increase in entropy and that the enthalpy of binding is approximately zero (Noy and Xu, 1990). These results were interpreted to indicate that binding is mainly stabilized by hydrophobic interactions, and that the hydroxyl moiety of retinol does not play a role in binding to RBP.An ideal method for study of chromophores embedded in proteins is resonance Raman spectroscopy. In this form of vibrational spectroscopy, the spectrum of a molecule is selectively probed by choosing an excitation light which overlaps the electronic absorption band of a chromophore. The resonantly enhanced Raman cross section is hence much larger than that of...

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Vibrational analysis of 13-cis-retinal

Cited by 71 publications

References 1 publication

Steric Constraint in the Primary Photoproduct of an Archaeal Rhodopsin from Regiospecific Perturbation of C−D Stretching Vibration of the Retinyl Chromophore

Steric Constraint in the Primary Photoproduct of an Archaeal Rhodopsin from Regiospecific Perturbation of C−D Stretching Vibration of the Retinyl Chromophore

The synthesis of 13C-labelled retinals

The interactions of retinoids with retinol‐binding protein

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