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PLANT PHYSIOLOGY , Vol 110, Issue 2 445-454, Copyright © 1996 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
Envelope Membranes from Spinach Chloroplasts Are a Site of Metabolism of Fatty Acid Hydroperoxides
E. Blee and J. Joyard
Institut de Biologie Moleculaire des Plantes (Centre National de la Recherche Scientifique [CNRS] Unite Propre de Recherche 406), Departement d'Enzymologie Cellulaire et Moleculaire, 28 rue Goethe, 67083 Strasbourg Cedex, France (E.B.)
Enzymes in envelope membranes from spinach (Spinacia oleracea L.)
chloroplasts were found to catalyze the rapid breakdown of fatty acid
hydroperoxides. In contrast, no such activities were detected in the stroma
or in thylakoids. In preparations of envelope membranes,
9S-hydroperoxy-10(E),12(Z)-octadecadienoic acid,
13S-hydroperoxy-9(Z),11(E)-octadecadienoic acid, or
13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid were transformed at
almost the same rates (1-2 [mu]mol min-1 mg-1 protein). The products formed
were separated by reversed-phase high-pressure liquid chromatography and
further characterized by gas chromatography-mass spectrometry. Fatty acid
hydroperoxides were cleaved (a) into aldehydes and oxoacid fragments,
corresponding to the functioning of a hydroperoxide lyase, (b) into ketols
that were spontaneously formed from allene oxide synthesized by a
hydroperoxide dehydratase, (c) into hydroxy compounds synthesized
enzymatically by a system that has not yet been characterized, and (d) into
oxoenes resulting from the hydroperoxidase activity of a lipoxygenase.
Chloroplast envelope membranes therefore contain a whole set of enzymes
that catalyze the synthesis of a variety of fatty acid derivatives, some of
which may act as regulatory molecules. The results presented demonstrate a
new role for the plastid envelope within the plant cell.
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