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- W2079702927 abstract "The photoreaction of vacuum-dried rhodopsin was monitored by UV-visible absorption spectroscopy. The results indicate that in dry rhodopsin, isorhodopsin and lumirhodopsin a protonation equilibrium exists between the protonated and the non-protonated Schiff base. On hydration the water stabilizes the protonated forms. In metarhodopsin-I the protein itself is able to stabilize the protonated Schiff base. The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O. The results are discussed with respect to the problem of charge stabilization and energy storage." @default.
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- W2079702927 date "1988-12-01" @default.
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- W2079702927 title "The photoreaction of vacuum-dried rhodopsin at low temperature: Evidence for charge stabilization by water" @default.
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- W2079702927 doi "https://doi.org/10.1016/1011-1344(88)85070-x" @default.
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