A quantitative model of odor deactivation based on the redox shift of the pheromone-binding protein im moth antennae.
Recent in vitro experiments with homogenates of isolated olfactory hairs of Antheraea polyphemus suggest that the pheromone-binding protein (PBP) is involved not only in pheromone solubilization and transport but also in pheromone deactivation. PBP occurs in a reduced form with one or two disulfide bridges (PBP(red)) and in the oxidized form with three bridges (PBP(ox)). From kinetic experiments it was concluded that the pheromone is first bound to PBP(red). This complex activates the receptor molecules and then turns into the oxidized form which--according to our working hypothesis--is unable to activate further receptor molecules. Apparently, the pheromone bound to the PBP (both forms) is protected from enzymatic degradation into nonexcitatory metabolites. A quantitative kinetic model of pheromone deactivation was developed (in collaboration with J. Thorson, Oxford) in which the receptor molecules are considered to act as enzymes catalyzing the redox shift of the binding protein.
Max-Planck-Institut für Verhaltenphysiologie Seewiesen, Starnberg, Germany. kaissling@mpi-seewiesen.mpg.de
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D000818:Animals; D002628:Chemoreceptor Cells / Q000378:metabolism*; D019476:Insect Proteins / Q000378:metabolism; D008954:Models, Biological; D009036:Moths; D009812:Odorants; D010084:Oxidation-Reduction; D010675:Pheromones / Q000378:metabolism*
D019476:Insect Proteins; D010675:Pheromones