Rhodopsin in Cell Membranes and the Process of Phototransduction

Montal, Mauricio; Korenbrot, Juan I.

doi:10.1007/978-1-4899-2693-7_13

Cited by 10 publications

(2 citation statements)

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“…Photoexcitation of rhodopsin leads to changes in the ion permeability of the outer segment plasma membrane, but the mechanism of this process remains unknown (Hagins, 1972;Montal & Korenbrot, 1976). We have recently reported (Korenbrot & Pramik, 1977) on an experimental approach to studying the function of rhodopsin that investigates the electrochemical properties of air-water interface films consisting of purified rhodopsin and phospholipids.…”

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confidence: 96%

Linear dichroism of rhodopsin in air-water interface films

Korenbrot

Jones

1979

J. Membrain Biol.

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Air-water interface films of purified cattle rhodopsin and defined phospholipids are formed by the osmotic lysis of reconstituted membrane vesicles. The interface films thus formed consist of a phospholipid monolayer containing vesicle membrane fragments. Rhodopsin molecules at the interface are restricted within the membrane fragments where they are spectrophotometrically intact and capable of undergoing photoregeneration and chemical regeneration. Multilayers of up to 8 layers can be built from these interface films. The visible absorption band of rhodopsin in these multilayers is linearly dichroic. Quantitative analysis of the linear dichroism reveals that the dipole moment of transition of the retinal chromophore in rhodopsin forms an angle of 15 degrees +/- 4 degrees with the plane of the membrane fragments in the interface film. This orientation of the chromophore relative to the plane of the membrane is essentially the same as that observed in the intact retina. Thus, the orientation of rhodopsin in the interface films is similar to that in the intact disc membranes.

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