Substituents at the C13 Position of Retinal and Their Influence on the Function of Bacteriorhodopsin

Paul Tavan; Klaus Schulten; Wolfgang Gärtner; Dieter Oesterhelt

doi:10.1016/S0006-3495(85)83925-4

Substituents at the C₁₃ Position of Retinal and Their Influence on the Function of Bacteriorhodopsin

Paul Tavan, Klaus Schulten, Wolfgang Gärtner, Dieter Oesterhelt

Physics

Research output: Contribution to journal › Article › peer-review

Abstract

Retinal analogues in which the 13-methyl group is replaced by H, C₂H₅, CF₃, and OCH₃ residues are studied by means of quantumchemical modified neglect of diatomic overlap-correlated version (MNDOC) calculations. The analogues are suitable to test the stereochemical mechanism of proton pumping in bacteriorhodopsin. The results explain the proton-pumping activities of bacterio-opsin reconstituted with these analogues and elucidate the decisive role of retinal's ground-state intramolecular properties in the pump cycle of bacteriorhodopsin.

Original language	English (US)
Pages (from-to)	349-355
Number of pages	7
Journal	Biophysical journal
Volume	47
Issue number	3
DOIs	https://doi.org/10.1016/S0006-3495(85)83925-4
State	Published - Jan 1 1985

ASJC Scopus subject areas

Biophysics

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abstract = "Retinal analogues in which the 13-methyl group is replaced by H, C2H5, CF3, and OCH3 residues are studied by means of quantumchemical modified neglect of diatomic overlap-correlated version (MNDOC) calculations. The analogues are suitable to test the stereochemical mechanism of proton pumping in bacteriorhodopsin. The results explain the proton-pumping activities of bacterio-opsin reconstituted with these analogues and elucidate the decisive role of retinal's ground-state intramolecular properties in the pump cycle of bacteriorhodopsin.",

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AU - Oesterhelt, Dieter

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AB - Retinal analogues in which the 13-methyl group is replaced by H, C2H5, CF3, and OCH3 residues are studied by means of quantumchemical modified neglect of diatomic overlap-correlated version (MNDOC) calculations. The analogues are suitable to test the stereochemical mechanism of proton pumping in bacteriorhodopsin. The results explain the proton-pumping activities of bacterio-opsin reconstituted with these analogues and elucidate the decisive role of retinal's ground-state intramolecular properties in the pump cycle of bacteriorhodopsin.

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