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- W2074328101 abstract "Abstract— Kinetic resonance Raman (RR) experiments were designed to study the time-behaviour of the retinal-binding protein bacteriorhodopsin (BR) in its photochemical cycle. The unphotolyzed chro-mophore B-570 and the two intermediates L-550 and M-412 were probed by the characteristic C=C stretching vibrations of the retinal moiety. Time resolution was achieved with a spinning cell as flow system in combination with two CW lasers in a pump-probe configuration. RR spectra were probed at 475 nm at various delay times between pump and probe event. The deconvolution of the spectra into the various components B-570, L-550 and M-412 was carried out by curve fitting procedures. It was found that at pH7.4 L-550 decays — with a time-constant of 62 μs — not completely but to a residual level of 35% of its initial value. This intermediate L-amplitude finally disappears in the ms-range (4.5 ms) synchroneously with the intermediate M-412. An analogeous time-behaviour was found at pH 4.6. In the basic range also an “L” -intermediate could be identified which is coupled to the long-lived M-component. To explain the peculiar time-dependence it is proposed that during the fast decay of L a dynamic equilibrium between L and M is established. Then during the reconstitution of B-570 the two intermediates disappear synchroneously. A molecular model is presented in which the dynamic equilibrium between L and M is explained by an oscillatory motion of a proton from the Schiff base group of the chromophore to its counterion." @default.
- W2074328101 created "2016-06-24" @default.
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- W2074328101 date "1986-01-01" @default.
- W2074328101 modified "2023-09-23" @default.
- W2074328101 title "TIME-RESOLVED RESONANCE RAMAN STUDIES ON THE PHOTOCHEMICAL CYCLE OF BACTERIORHODOPSIN" @default.
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- W2074328101 doi "https://doi.org/10.1111/j.1751-1097.1986.tb05591.x" @default.
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