Studies on cephalopod rhodopsin: photoisomerization of the chromophore

Biochim Biophys Acta. 1976 Apr 23;428(2):321-38. doi: 10.1016/0304-4165(76)90040-4.

Abstract

Photoisomerization of the chromophore of squid rhodopsin is dependent upon the irradiation temperature. Above 0 degrees C, only 11-cis in equilibrium all-trans reaction proceeds and the all-trans leads to 9-cis reaction is limited to extremely low efficiency. At liquid nitrogen temperature, 11 cis in equilibrium all-trans in equilibrium 9-cis reaction takes place. At intermediary low temperatures (-80 degrees C to -15 degrees C) another isomer of retinal may be produced by the irradiation, which forms a pigment having an absorbance maximum at 465 nm (P-465). The formation of P-465 decreases remarkably in the narrow temperature range from -30 degrees C to 0 degrees C where mesorhodopsin converts to metarhodopsin. Medsorhodopsin is quite different from metarhodopsin in the photoisomerization of the chromophore because P-465 is produced from the former but not from the latter. No P-465 is produced both at liquid nitrogen temperature and above 0 degrees C. P-465 is more labile than any of the other photoproducts so far known, that is isorhodopsin, alkaline and acid metarhodopsins. P-465 is converted to metarhodopsin by irradiation.

MeSH terms

  • Animals
  • Circular Dichroism
  • Decapodiformes
  • Isomerism
  • Mathematics
  • Photochemistry
  • Protein Conformation
  • Retinal Pigments*
  • Rhodopsin*
  • Spectrophotometry
  • Spectrophotometry, Ultraviolet
  • Temperature

Substances

  • Retinal Pigments
  • Rhodopsin