Enantioselective binding of an 11-cis-locked cyclopropyl retinal. The conformation of retinal in bovine rhodopsin.
[formula: see text] The conformation of the retinal chromophore in rhodopsin is central for understanding the visual transduction process. The absolute twist around the 12-s bond of the chromophore in rhodopsin has been determined by studies with 11-cis-locked 11,12-cyclopropylretinal analogues (11S,12R)-2 and (11R,12S)-3, enantioselectively synthesized with the aid of an enzyme. The finding that enantiomer 2 binds to opsin while the other 3 does not defines the absolute sense of twist around the 12-s bond.
Lou
J
J
Department of Chemistry, Columbia University, New York, New York 10027, USA.
Hashimoto
M
M
Berova
N
N
Nakanishi
K
K
D000818:Animals; D001643:Bridged Bicyclo Compounds / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D012172:Retinaldehyde / Q000031:analogs & derivatives* / Q000737:chemistry*; D012243:Rhodopsin / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013237:Stereoisomerism
C410325:4-(2-((1,3,3-trimethylcyclohexen-2-yl)ethenyl)propylidene)-2,3-methylenecyclohept-1-ylmethylenemethanal; D001643:Bridged Bicyclo Compounds; D012243:Rhodopsin; D012172:Retinaldehyde