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The Nature of the Delocalized Cations in Azulenic Bacteriorhodopsin Analogs ¶

Depending on the size and shape of their azulenic chromophores, azulenic bacteriorhodopsin (bR) pigment analogs can exist as either an initial pigment P1, a more red‐shifted final pigment P2 or an equilibrium mixture of both. The absorption spectra of red‐shifted bR analogs exhibit characteristic narrow‐band shapes similar to charge fully delocalized cyanine‐like dyes. Therefore, all such red‐shifted pigments are believed to be highly delocalized, bond‐equalized carbocations. We have determined structural requirements that facilitate their formation. To describe fully the red‐shift potentials of these retinal analogs, we have introduced a new parameter—percent red‐shift (PRS). A large PRS value not only reflects the extent of red‐shift, but is also suggestive of extensive delocalization of the positive charge. Relevance of these findings in consideration of the possibility of forming stable O‐intermediates is presented. The postulated resonance hybrid‐like structures for different cations of the positively charged protonated Schiff base chromophores are in fact structurally distinct species, equilibrating in response to local perturbations within the supramolecular protein environment.