Fig. 7: The multi-exponential decay of the K intermediate. | Nature Communications

Fig. 7: The multi-exponential decay of the K intermediate.

From: Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct

Fig. 7

A The C=C bond relaxation pathway from Franck-Condon (FC) to alternate bond-lengths (ABL) in the 13-cis, 15-anti K intermediate of AT-BR (all-trans Bacteriorhodopsin). The CASPT2//CASSCF/MM minimum energy paths (MEPs) of the FC→ABL in three different conformations of the carboxylic acid group of protonated ASP212, i.e., B OD1s, syn conformation-O1 protonated, C OD2s, syn conformation-O2 protonated and D OD1a, anti conformation-O1 protonated. The values 0.18, 2.97 and 6.45 kcal mol−1 are associated with the energy barriers along the C=C bond relaxation path of OD1s, OD2s, and OD1a, respectively. Source data are provided as a Source Data file.

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