Haemoprotein- and transition metal ion-catalysed oxidation of linoleic acid. Selectivity of the position of oxygenation.
Oxidation of linoleic acid in aqueous buffers favoured the formation of the 13 positional isomers of hydroperoxylinoleic acid. The reaction which was catalysed by haemoproteins and Fe(II) and Cu(II) ions showed positional selectivity that was similar to lipoxygenase-catalysed reactions but yielded equal proportions of both enantiomers of the hydroperoxides. There was little selectivity when methyl linoleate was used as the substrate or when linoleic acid was oxidised in organic solvents. The results indicated that positional selectivity was, at least in part, due to the conformation of the fatty acid molecule in aqueous media. Implication of the selectivity in a non-enzymic reaction is discussed especially in relation to its effect on the determination of lipoxygenase specificities.
D002021:Buffers; D003300:Copper / Q000494:pharmacology; D006420:Hemeproteins; D007501:Iron / Q000494:pharmacology; D008041:Linoleic Acids / Q000378:metabolism; D008628:Mercury / Q000494:pharmacology; D008968:Molecular Conformation; D008982:Molybdenum / Q000494:pharmacology; D010084:Oxidation-Reduction; D011136:Polysorbates; D013237:Stereoisomerism
D002021:Buffers; D006420:Hemeproteins; D008041:Linoleic Acids; D011136:Polysorbates; D003300:Copper; D008982:Molybdenum; D007501:Iron; D008628:Mercury; C032890:13-hydroperoxylinoleic acid