Chloroplast-Diphenyl Ether Interactions II
Author(s) -
Scott H. Wettlaufer,
Ruth Alscher,
Christine A. Strick
Publication year - 1985
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.78.2.215
Subject(s) - chloroplast , chloroplast stroma , biochemistry , ferredoxin , dithiothreitol , dehydrogenase , thioredoxin , fructose 1,6 bisphosphatase , glyceraldehyde 3 phosphate dehydrogenase , stroma , biology , ferredoxin thioredoxin reductase , chemistry , photosynthesis , fructose , enzyme , thioredoxin reductase , thylakoid , immunohistochemistry , gene , immunology
Acifluorfen, a p-nitrodiphenyl ether herbicide, is inhibitory to those photosynthetic functions that require a functioning chloroplast envelope. Functions involving the stroma are also affected. Acifluorfen does not lyse intact spinach chloroplasts, yet does increase the sensitivity of CO(2)-dependent O(2) evolution to exogenous inorganic phosphate without directly affecting the function of the phosphate translocator. Acifluorfen penetrates into the chloroplast stroma in a light-independent fashion. Once inside, it causes the inactivation of light and dithiothreitol-activated fructose 1,6-bisphosphatase. Light-activated glyceraldehyde-3-phosphate dehydrogenase (NADP) is also inactivated by acifluorfen.These data suggest that acifluorfen stimulates a pathway for inactivation of fructose 1,6-bisphosphatase and glyceraldehyde 3-phosphate dehydrogenase (NADP) which uses oxygen as a terminal oxidant and which involves thioredoxin and ferredoxin-thioredoxin reductase.
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