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Oxyfluorfen and Lipid Peroxidation: Protein Damage as a Phytotoxic Consequence

Published online by Cambridge University Press:  12 June 2017

Karl J. Kunert
Affiliation:
Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-775 Konstanz, West Germany
Carmen Homrighausen
Affiliation:
Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-775 Konstanz, West Germany
Herbert Böhme
Affiliation:
Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-775 Konstanz, West Germany
Peter Böger
Affiliation:
Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-775 Konstanz, West Germany

Abstract

Protein damage, as a primary phytotoxic consequence of in vivo lipid peroxidation, induced by the diphenyl ether herbicide oxyfluorfen [2-chloro-1-(3-ethoxy-4-nitrophenoxy)-4-(trifluoromethyl)benzene] at a concentration of 10 μM, was measured with the green alga Scenedesmus acutus. In the light, water-soluble proteins are destroyed by a herbicide-induced peroxidation process that can be detected by production of fluorescent products and loss of specific amino acid residues of proteins. The water-soluble cytochrome c-553 and the membrane-bound cytochrome f-553, components of the photosynthetic electron transport, were specifically used as sensitive markers for protein damage, measured as decrease of redox reactions of the cytochromes. Under peroxidizing conditions, destruction of the algal cytochrome c is significantly higher than destruction of membrane-bound components, such as cytochrome f and chlorophyll. Protection against protein loss is achieved by the nonbiological antioxidant ethoxyquin (1,2-dihydro-6-ethoxy-2,2,4-trimethylquinoline) or the photosynthesis inhibitor diuron [N′-(3,4-dichlorophenyl)-N,N-dimethylurea].

Type
Physiology, Chemistry, and Biochemistry
Copyright
Copyright © 1985 by the Weed Science Society of America 

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