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Protein-induced bonding perturbation of the rhodopsin chromophore detected by double-quantum solid-state NMR

Protein-induced bonding perturbation of the rhodopsin chromophore detected by double-quantum solid-state NMR
Protein-induced bonding perturbation of the rhodopsin chromophore detected by double-quantum solid-state NMR
We have obtained carbon-carbon bond length data for the functional retinylidene chromophore of rhodopsin, with a spatial resolution of 3 pm. The very high resolution was obtained by performing double-quantum solid-state NMR on a set of noncrystalline isotopically labelled bovine rhodopsin samples. We detected localized perturbations of the carbon-carbon bond lengths of the retinylidene chromophore. The observations are consistent with a model in which the positive charge of the protonated Schiff base penetrates into the polyene chain and partially concentrates around the C13 position. This coincides with the proximity of a water molecule located between the glutamate-181 and serine-186 residues of the second extracellular loop, which is folded back into the transmembrane region. These measurements support the hypothesis that the polar residues of the second extracellular loop and the associated water molecule assist the rapid selective photoisomerization of the retinylidene chromophore by stabilizing a partial positive charge in the center of the polyene chain.
coupled-receptor rhodopsin, molecular torsional angle, protonated schiff-base, mas nmr, retinylidene chromophore, counterion switch, crystal-structure, metarhodopsin-i, ionone ring, 1st step
0002-7863
3948-3953
Carravetta, Marina
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Zhao, Xin
634e60cd-764f-48ab-9759-673fe78842d4
Johannessen, Ole G.
799ccc8c-a2e7-4305-a03a-2dc9f42564ef
Lai, Wai C.
86470f61-cbff-41d4-bb9b-ec0b02af1552
Verhoeven, Michiel A.
94b2c838-a88e-4388-8f2c-3788dbcb1f76
Bovee-Geurts, Petra H.M.
66d6099e-73b5-4f84-ae7a-2b61d874e4e9
Verdegem, Peter J.E.
72ab5611-e197-4750-9cbd-a7cdee83d67e
Kiihne, Suzanne
23bb8dab-08b0-4e1c-8ff1-10f6a476e560
Luthman, Henrik
662dcf74-bbdd-49d2-bac2-b84304eea393
de Groot, Huub J.M.
3b161258-7c2a-431f-aab4-004636d50c68
deGrip, William J.
90b1364c-58bf-4a50-95b1-0711542ea5af
Lugtenburg, Johan
b920f5ab-0138-479f-88b1-f4bca6b32dad
Levitt, Malcolm H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3
Carravetta, Marina
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Zhao, Xin
634e60cd-764f-48ab-9759-673fe78842d4
Johannessen, Ole G.
799ccc8c-a2e7-4305-a03a-2dc9f42564ef
Lai, Wai C.
86470f61-cbff-41d4-bb9b-ec0b02af1552
Verhoeven, Michiel A.
94b2c838-a88e-4388-8f2c-3788dbcb1f76
Bovee-Geurts, Petra H.M.
66d6099e-73b5-4f84-ae7a-2b61d874e4e9
Verdegem, Peter J.E.
72ab5611-e197-4750-9cbd-a7cdee83d67e
Kiihne, Suzanne
23bb8dab-08b0-4e1c-8ff1-10f6a476e560
Luthman, Henrik
662dcf74-bbdd-49d2-bac2-b84304eea393
de Groot, Huub J.M.
3b161258-7c2a-431f-aab4-004636d50c68
deGrip, William J.
90b1364c-58bf-4a50-95b1-0711542ea5af
Lugtenburg, Johan
b920f5ab-0138-479f-88b1-f4bca6b32dad
Levitt, Malcolm H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3

Carravetta, Marina, Zhao, Xin, Johannessen, Ole G., Lai, Wai C., Verhoeven, Michiel A., Bovee-Geurts, Petra H.M., Verdegem, Peter J.E., Kiihne, Suzanne, Luthman, Henrik, de Groot, Huub J.M., deGrip, William J., Lugtenburg, Johan and Levitt, Malcolm H. (2004) Protein-induced bonding perturbation of the rhodopsin chromophore detected by double-quantum solid-state NMR. Journal of the American Chemical Society, 126 (12), 3948-3953. (doi:10.1021/ja039390q).

Record type: Article

Abstract

We have obtained carbon-carbon bond length data for the functional retinylidene chromophore of rhodopsin, with a spatial resolution of 3 pm. The very high resolution was obtained by performing double-quantum solid-state NMR on a set of noncrystalline isotopically labelled bovine rhodopsin samples. We detected localized perturbations of the carbon-carbon bond lengths of the retinylidene chromophore. The observations are consistent with a model in which the positive charge of the protonated Schiff base penetrates into the polyene chain and partially concentrates around the C13 position. This coincides with the proximity of a water molecule located between the glutamate-181 and serine-186 residues of the second extracellular loop, which is folded back into the transmembrane region. These measurements support the hypothesis that the polar residues of the second extracellular loop and the associated water molecule assist the rapid selective photoisomerization of the retinylidene chromophore by stabilizing a partial positive charge in the center of the polyene chain.

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Published date: 31 March 2004
Keywords: coupled-receptor rhodopsin, molecular torsional angle, protonated schiff-base, mas nmr, retinylidene chromophore, counterion switch, crystal-structure, metarhodopsin-i, ionone ring, 1st step

Identifiers

Local EPrints ID: 20161
URI: http://eprints.soton.ac.uk/id/eprint/20161
ISSN: 0002-7863
PURE UUID: 9432971e-80f6-4280-8751-a736cdb32265
ORCID for Marina Carravetta: ORCID iD orcid.org/0000-0002-6296-2104
ORCID for Malcolm H. Levitt: ORCID iD orcid.org/0000-0001-9878-1180

Catalogue record

Date deposited: 22 Feb 2006
Last modified: 18 Feb 2021 16:59

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Contributors

Author: Xin Zhao
Author: Ole G. Johannessen
Author: Wai C. Lai
Author: Michiel A. Verhoeven
Author: Petra H.M. Bovee-Geurts
Author: Peter J.E. Verdegem
Author: Suzanne Kiihne
Author: Henrik Luthman
Author: Huub J.M. de Groot
Author: William J. deGrip
Author: Johan Lugtenburg

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