Circular dichroism of cattle rhodopsin and bathorhodopsin at liquid nitrogen temperatures

Abstract

The photoevent in vision has been considered to be the conversion of rhodopsin to bathorhodopsin, which is caused by photoisomerization of the chromphoric retinal. Recently some objections were raised to this hypothesis. The reliability of the hypothesis was verified by measurement of circular dichroism of bathorhodopsin. The measurement of circular dichroism of rhodopsin extract (containing 66% or 75% of glycerol) at liquid nitrogen temperatures (-195 degrees C) by a conventional spectropolarimeter induced an extraordinary large signal, owing to linear dichroism originated from conversion of rhodopsin to bathorhodopsin by the measuring light. The similar linear dichrolism can be induced by irradiation of rhodopsin extract at -195 degrees C with polarized light or natural light. At photosteady state the linear dichroism disappeared. Circular dichroism spectrum of cattle rhodopsin displayed two positive peaks ([theta]max = 80 800 degrees at 335 nm, and [theta]max = 42 600 degrees at 500 nm) at -195 degrees C, whereas, bathorhodopsin displayed a positive peak ([theta]max = 43 100 degrees at 334 nm) and a negative peak ([theta]max = 163 000 degrees at 540 nm). The change of the positive sign to negative one at alpha-band of circular dichroism spectrum supports the hypothesis that the conversion of rhodopsin is due to rotation of the chromophoric retinal about C-11--12 double bond ('photoisomerization model').