Interrelations of bioenergetic and sensory functions of the retinal proteins.
Rhodopsins are intrinsic membrane retinal-containing proteins composed of 7 hydrophobic alpha-helical transmembrane columns and hydrophilic sequences of various length connecting the helices and localized at N- and C-ends of the polypeptide. The chromophore (retinal) forms a Schiff base with a lysine residue in the middle part of the last alpha-helix. Absorption of a photon results in isomerization of retinal which gives rise to a conformational change in the protein moiety. Rhodopsins can be involved in two entirely different types of activities, i.e. ion pumping and photosensing. Recent observations concerning the pumping and sensory mechanisms allowed both these events to be explained in terms of one and the same unitary concept, which postulates the formation of a hydrophilic cleft in the hydrophobic part of the protein molecule as a crucial step in energy conservation and photosensing.
Skulachev
V P
VP
Department of Bioenergetics, A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
D000818:Animals; D001436:Bacteriorhodopsins / Q000502:physiology*; D004734:Energy Metabolism / Q000502:physiology*; D005136:Eye Proteins / Q000502:physiology*; D019617:Halobacterium salinarum / Q000502:physiology*; D009419:Nerve Tissue Proteins / Q000502:physiology*; D012160:Retina
D005136:Eye Proteins; D009419:Nerve Tissue Proteins; D001436:Bacteriorhodopsins