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On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin.

The kinetics of formation of both the tyrosinate ion (from its absorption at 296 nm) and the deprotonated Schiff base (M412) (from its absorption at 404 nm) are studied simultaneously at different pH values (7-11) and temperatures (5-25 degrees C). Two formation rates are observed for M412 in agreement with previous observations. The slow one is dominant under physiological conditions and is found to be slightly faster than that for the tyrosinate formation. This is in disagreement with the proposal that the tyrosinate formation is a prerequisite to the deprotonation of the Schiff base (M412). The ratio of the amplitudes of the fast and slow components is found to be sensitive to pH and, at any pH, it can be used to calculate an amino acid pKa value of 9.6. This is explained by proposing the existence of two sites for the protonated Schiff base within the protein. In one site, the Schiff base is near the neutral form of an amino acid residue with a pKa value of 9.6 (giving rise to the slow component), while in the other, it is near its conjugate base. The formation of the tyrosinate ion as well as the formation of the slow and fast components of M412 all have activation energies that are comparable to H-bond energies. A model is suggested to account for this and the comparable deprotonation rates of tyrosine and the slow component of the protonated Schiff base. It involves the reduction of their pKa by their exposure to a positively charged species.