A pigment made up of a protein able to bind retinal as well as retinol is described. The molecule consists of a dimer with a molecular weight of 50,000 which binds one molecule of retinal. The binding site for retinal is a Schiff base buried in the interior of the protein. Retinol is probably bound to the protein in the same site as for retinal, although not covalently, as suggested by the absorbance spectra. The protein, extracted from honeybee retina, is involved in visual pigment metabolism (1), and its structure may elucidate the mechanism of the stereospecific photoisomerization of all trans-retinal to 11-cis-retinal. © 1987 Humana Press Inc.
Structure of a protein catalyzing the formation of 11 cis-retinal in the visual cycle of invertebrate eyes
Pepe I. M.;Vergani L.;
1987-01-01
Abstract
A pigment made up of a protein able to bind retinal as well as retinol is described. The molecule consists of a dimer with a molecular weight of 50,000 which binds one molecule of retinal. The binding site for retinal is a Schiff base buried in the interior of the protein. Retinol is probably bound to the protein in the same site as for retinal, although not covalently, as suggested by the absorbance spectra. The protein, extracted from honeybee retina, is involved in visual pigment metabolism (1), and its structure may elucidate the mechanism of the stereospecific photoisomerization of all trans-retinal to 11-cis-retinal. © 1987 Humana Press Inc.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
