A unifying concept for ion translocation by retinal proteins.
First, halorhodopsin is capable of pumping protons after illumination with green and blue light in the same direction as chloride. Second, mutated bacteriorhodopsin where the proton acceptor Asp85 and the proton donor Asp96 are replaced by Asn showed proton pump activity after illumination with blue light in the same direction as wildtype after green light illumination. These results can be explained by and are discussed in light of our new hypothesis: structural changes in either molecule lead to a change in ion affinity and accessibility for determining the vectoriality of the transport through the two proteins.
Oesterhelt
D
D
Max-Planck-Institu für Biochemie, Martinsried, Germany.
Tittor
J
J
Bamberg
E
E
D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism*; D001692:Biological Transport; D025602:Halorhodopsins; D007477:Ions; D008954:Models, Biological; D008969:Molecular Sequence Data
D025602:Halorhodopsins; D007477:Ions; D001436:Bacteriorhodopsins