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Resonance Raman Analysis of the Mechanism of Energy Storage and Chromophore Distortion in the Primary Visual Photoproduct

Biochemistry (Easton), 2004-08, Vol.43 (34), p.10867-10876 [Peer Reviewed Journal]

Copyright © 2004 American Chemical Society ;ISSN: 0006-2960 ;ISSN: 0021-9258 ;EISSN: 1520-4995 ;EISSN: 1083-351X ;DOI: 10.1021/bi0400148 ;PMID: 15323547

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Title:
Resonance Raman Analysis of the Mechanism of Energy Storage and Chromophore Distortion in the Primary Visual Photoproduct
Author: Yan, Elsa C. Y ; Ganim, Ziad ; Kazmi, Manija A ; Chang, Belinda S. W ; Sakmar, Thomas P ; Mathies, Richard A
Subjects: Animals ; BASIC BIOLOGICAL SCIENCES ; BIOCHEMISTRY ; Cattle ; ENERGY STORAGE ; Freezing ; Glutamic Acid - genetics ; Light ; Models, Molecular ; Mutagenesis, Site-Directed ; national synchrotron light source ; Photochemistry ; Protein Conformation ; Protein Structure, Secondary ; Protons ; RESONANCE ; Rhodopsin - analogs & derivatives ; Rhodopsin - chemistry ; Rhodopsin - genetics ; Rhodopsin - metabolism ; Schiff Bases - chemistry ; Serine - genetics ; Species Specificity ; Spectrum Analysis, Raman - methods ; Static Electricity ; Thermodynamics
Is Part Of: Biochemistry (Easton), 2004-08, Vol.43 (34), p.10867-10876
Description: The vibrational structure of the chromophore in the primary photoproduct of vision, bathorhodopsin, is examined to determine the cause of the anomalously decoupled and intense C11C12 hydrogen-out-of-plane (HOOP) wagging modes and their relation to energy storage in the primary photoproduct. Low-temperature (77 K) resonance Raman spectra of Glu181 and Ser186 mutants of bovine rhodopsin reveal only mild mutagenic perturbations of the photoproduct spectrum suggesting that dipolar, electrostatic, or steric interactions with these residues do not cause the HOOP mode frequencies and intensities. Density functional theory calculations are performed to investigate the effect of geometric distortion on the HOOP coupling. The decoupled HOOP modes can be simulated by imposing ∼40° twists in the same direction about the C11C12 and C12−C13 bonds. Sequence comparison and examination of the binding site suggests that these distortions are caused by three constraints consisting of an electrostatic anchor between the protonated Schiff base and the Glu113 counterion, as well as steric interactions of the 9- and 13-methyl groups with surrounding residues. This distortion stores light energy that is used to drive the subsequent protein conformational changes that activate rhodopsin.
Publisher: United States: American Chemical Society
Language: English
Identifier: ISSN: 0006-2960
ISSN: 0021-9258
EISSN: 1520-4995
EISSN: 1083-351X
DOI: 10.1021/bi0400148
PMID: 15323547
Source: MEDLINE
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Resonance Raman Analysis of the Mechanism of Energy Storage and Chromophore Distortion in the Primary Visual Photoproduct

Copyright © 2004 American Chemical Society ;ISSN: 0006-2960 ;ISSN: 0021-9258 ;EISSN: 1520-4995 ;EISSN: 1083-351X ;DOI: 10.1021/bi0400148 ;PMID: 15323547

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