Search results for "Acifluorfen"

showing 7 items of 7 documents

Kinetic studies on protoporphyrinogen oxidase inhibition by diphenyl ether herbicides

1991

Diphenyl ethers (DPEs) and related herbicides are powerful inhibitors of protoporphyrinogen oxidase, an enzyme involved in the biosynthesis of haems and chlorophylls. The inhibition kinetics of protoporphyrinogen oxidase of various origins by four DPEs, (methyl)-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (acifluorfen and its methyl ester, acifluorfen-methyl), methyl-5-[2-chloro-4-(trifluoromethyl) phenoxy]-2-chlorobenzoate (LS 820340) and methyl-5-[2-chloro-5-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (RH 5348), were studied. The inhibitions of the enzymes from maize (Zea mays) mitochondrial and etiochloroplastic membranes and mouse liver mitochondrial membranes were com…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]Carboxylic acidMitochondria LiverEtherSaccharomyces cerevisiaeAcifluorfen01 natural sciencesBiochemistryMitochondrial ProteinsMiceStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEPhenolsAnimalsProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesTrifluoromethylFlavoproteinsHerbicidesDiphenyl etherIntracellular MembranesCell BiologyPlantsMitochondriaProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryProtoporphyrinogen oxidaseOxidoreductasesEthersResearch Article010606 plant biology & botanyBiochemical Journal
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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Synthesis and properties of a photoaffinity labeling reagent for protoporphyrinogen oxidases, the target enzymes of diphenyl ether herbicides

1994

A diazoketone 3 has been synthesized in two steps from acifluorfen 1, a diphenyl ether herbicide. Like the parent compound 1, the diazoketone 3 is toxic to plant cells and inhibits protoporphyrinogen oxidase, the molecular target of diphenyl ether herbicides. On photolysis of 3 in methanol, the generated carbene mainly undergoes the Wolff rearrangement to a ketene which further adds methanol, but many other products are observed. A tritiated derivative of 3 has been prepared which is suitable for photoaffinity labeling experiments.

0106 biological sciencesOxidoreductases Acting on CH-CH Group Donors[SDV]Life Sciences [q-bio]Clinical BiochemistryPharmaceutical ScienceKeteneAcifluorfen01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundDrug DiscoveryOrganic chemistryProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesPhotolysisPhotoaffinity labelingMolecular StructureBIOCHIMIEHerbicidesOrganic ChemistryDiphenyl etherWolff rearrangementAffinity Labels[SDV] Life Sciences [q-bio]chemistryTOXICOLOGIEReagentMolecular MedicineProtoporphyrinogen oxidaseIndicators and ReagentsMethanolSoybeansOxidoreductases010606 plant biology & botany
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Effects of Acifluorfen-methyl on cucumber cotyledons : porphyrin accumulation

1988

Abstract The nitrodiphenyl ether herbicide acifluorfen-methyl and the pyridine derivative LS 82-556 induce porphyrin accumulation in green cucumber cotyledons. When experiments are done with intact plants absorbing the herbicide through the roots, that accumulation is light-dependent. 3-(3,4-Dichlorophenyl)-1,1-dimethylurea (DCMU) which prevents cellular damages under these conditions (M. Matringe and R. Scalla, Pestic. Biochem. Physiol. 26 , 150 (1986), also inhibits porphyrin accumulation. In contrast, when detached cotyledons are cut into pieces and floated on herbicide solutions, porphyrins accumulate in the dark. Accordingly, DCMU does not inhibit porphyrin accumulation or protect the …

0106 biological sciencesfood.ingredientHealth Toxicology and Mutagenesis[SDV]Life Sciences [q-bio]Acifluorfen01 natural sciences03 medical and health scienceschemistry.chemical_compoundfoodBiosynthesispolycyclic compoundsPHOSPHYRINEComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesfood and beveragesDCMUBiological activityGeneral MedicineMetabolismPorphyrin[SDV] Life Sciences [q-bio]ChloroplastchemistryBiochemistryAgronomy and Crop ScienceCotyledon010606 plant biology & botany
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Off-line solid-phase microextraction and capillary electrophoresis mass spectrometry to determine acidic pesticides in fruits.

2003

A method based on solid-phase microextraction (SPME) and capillary electrophoresis/mass spectrometry (CE/ MS) is described for determining simultaneously five acidic pesticides (o-phenylphenol, ioxynil, haloxyfop, acifluorfen, picloram) in fruits. The CE device is coupled to an electrospray interface by a commercial sheath-flow adapter. Emphasis is placed on fulfillment of the speed and sensitivity requirements. The best separation is achieved using 32 mM ammonium formate/acid formic buffer at pH 3.1, with a working voltage of 25 kV. The MS detection of the five pesticides was performed in negative ionization mode. Full-scan spectra with base peaks corresponding to [M-H]- were obtained exce…

Detection limitChromatographyChemistryPlant ExtractsAnalytical chemistryElectrophoresis CapillaryFood ContaminationAcifluorfenMass spectrometrySolid-phase microextractionCapillary electrophoresis–mass spectrometryMass SpectrometryAnalytical Chemistrychemistry.chemical_compoundCapillary electrophoresisFruitAmmonium formateSample preparationPesticidesAnalytical chemistry
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Competitive interaction of three peroxidizing herbicides with the binding of 3H acifluorfen to corn etioplast membranes

1990

AbstractThe specific binding of the herbicide acifluorfen 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid to corn etioplast membranes is competitively inhibited by protoporphyrinogen IX, the substrate of protoporphyrinogen oxidase. Three other peroxidizing molecules, oxadiazon [5-ter-butyl-3-(2,4-dichloro-5-isopropoxyphenyl)-1,3,4-oxadiazol-2-one], LS 82556 [(S)3-N-(methylbenzyl)carbamoyl-5-propionyl-2,6-lutidine], and M&B 39279 [5-amino-4-cyano-1-(2,6-dichloro-4-trifluoromethylphenyl)pyrazol], also compete with acifluorfen for its binding site. The four herbicides thus bind to the same site, or to closely located sites, on the enzyme protoporphyrinogen oxidase.

Niacinamide0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistryBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyAcifluorfenBinding CompetitiveZea mays01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundEtioplastStructural BiologyDiphenyletherGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOxadiazoles0303 health sciencesBinding SitesTrifluoromethylHerbicidesCell MembraneCell BiologyPlantsBindingProtoporphyrinogen IXProtoporphyrinogen oxidaseEnzymeMembranechemistryDiuronNitrobenzoatesPyrazolesProtoporphyrinogen oxidaseHerbicideOxidoreductases010606 plant biology & botany
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Synthesis of tritiated derivatives of the diphenylether herbicides acifluorfen and acifluorfen methyl

1992

Acifluorfen 1 and acifluorfen methyl 2, two herbicides of the diphenylether family, are inhibitors of protoporphyrinogen oxidases. Two tritiated derivatives of these compounds, namely 3-[3H]-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid [3H]-1, and methyl 3-[3H]-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid [3H]-2, have been synthesised from 3-[3H]-5-hydroxybenzoic acid, in order to probe their interactions with the target enzymes.

Stereochemistry[SDV]Life Sciences [q-bio]Nitro compoundEtherAcifluorfenBiochemistryAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEDrug DiscoveryPIPHENYL ETHERRadiology Nuclear Medicine and imagingSYNTHESESpectroscopyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesTrifluoromethyl030302 biochemistry & molecular biologyOrganic Chemistry3. Good health[SDV] Life Sciences [q-bio]Enzyme inhibitionEnzymeAcifluorfen-methylchemistryProtoporphyrinogen oxidaseCHIMIE ORGANIQUE
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