Abstract
The molecular mechanism(s) by which bacteriorhodopsin (BR) utilizes the radiative energy in the visible region absorbed by the retinal chromophore is of major importance in characterizing the bacterial photocycle and the associated transport of protons across the BR membrane. The changes in retinal structure, electronic properties, and conformation which occur within the first 100 ps following excitation are examined here using time-resolved resonance Raman (TR3) and fluorescence (TRF) spectroscopies with 5 ps time resolution. TR3 spectra identify at least one major change in retinal structure (all-trans to 13-cis isomerization) occurring during the first 40 ps of the reaction, while TRF spectra reveal previously unreported fluorescence from a BR intermediate. These TR3 and TRF data are used to construct a model for retinal dynamics over the initial 100 ps interval of the BR photocycle.KeywordsProbe LaserEmission YieldTrans RetinalPhotochemical Quantum YieldRetinal ChromophoreThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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