Abstract
Abstract 13-Hydroperoxy-9cis,12trans-octadecadienoic acid (13-LOOH) reacts with methionine and methionine-containing peptides in absence of any other reagent by slow release of ethylene. Ethylene was identified by mass spectrometry and quantified by gas chromatography. The amount of ethylene released in a certain time interval depends on the position of the methionine residue in the peptide chain. Highest rates of ethylene release were measured with peptides carrying methionine at the N-terminus. 13-Hydroperoxy-9cis,12trans-octadecadie-noic acid can be substituted by linoleic acid, lipoxigenase and oxygen. We assume that the instant formation of lipid peroxides after plant injury and the instant release of ′wound ethylene′ are related. Since the initiator tRNA in eucaryontic cells always carries a methionine, all newly produced proteins contain methionine at the N-terminal position and are therefore sensitive to oxidative damage by hydroperoxides of fatty acids.
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