Effect of salt on the tyrosine and protonated Schiff base deprotonation kinetics in bacteriorhodopsin

Abstract

It is observed that the number of protons pumped per M412 formed in the bacteriorhodopsin photocycle almost doubles at high salt concentrations. In this paper, we studied the rates of deprotonation of tyrosine and of the two components of the protonated Schiff base at high salt concentrations, and at different pHs and temperatures. It is found that at pH = 7, increasing the salt concentration decreases the rates of deprotonation of the protonated Schiff base and tyrosine. This strongly suggests that the observed gain in the quantum yield of proton release per M412 formed when the salt concentration is increased is not a result of an increase in these rates. However, at high pH, e.g. 9.6, increasing the salt concentration increases the rate of deprotonation of the Schiff base by about 50%. Under all conditions, the slow component of the Schiff base is found to lose its proton prior to tyrosine.