Enantioselective binding of an 11-cis-locked cyclopropyl retinal. The conformation of retinal in bovine rhodopsin

Org Lett. 1999 Jul 15;1(1):51-4. doi: 10.1021/ol990048l.

Abstract

[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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bridged Bicyclo Compounds / chemistry*
  • Cattle
  • Circular Dichroism
  • Models, Molecular
  • Molecular Conformation
  • Protein Binding
  • Retinaldehyde / analogs & derivatives*
  • Retinaldehyde / chemistry*
  • Rhodopsin / chemistry*
  • Spectrophotometry, Ultraviolet
  • Stereoisomerism

Substances

  • 4-(2-((1,3,3-trimethylcyclohexen-2-yl)ethenyl)propylidene)-2,3-methylenecyclohept-1-ylmethylenemethanal
  • Bridged Bicyclo Compounds
  • Rhodopsin
  • Retinaldehyde