When anesthetics were added to a bacteriorhodopsin (bR) in the purple membranes, the 570 nm absorption band shifts to 480 nm. This anesthetic-induced spectroscopic change is reversible. The apparent pKa (6.3) of this equilibrium depends on the nature of the anesthetics in which bR is dispersed. The electric orientation measurements showed that the native bR is easily achieved by relatively small electric field which is oriented at $60^circ$, while anesthetic-treated bR is not the case. These results demonstrate that the subtle changes in the chromophore and the protein structure surrounding the chromophore by anesthetics influence the spatial orientation of the charged residues in the protein matrix surrounding chromophore.