0000000000622714

AUTHOR

Michel Matringe

showing 17 related works from this author

Effects of peroxidizing herbicides on protoporphyrin IX levels in non-chlorophyllous soybean cell culture

1990

Abstract The mode of action of 16 peroxidizing herbicides belonging to four different families (diphenyl ethers, oxadiazon, pyridine derivatives, and pyrazole derivatives) has been studied in nonchlorophyllous soybean cell cultures. Whenever possible, we have compared active and inactive compounds. Phytotoxic effects were estimated on the basis of growth inhibition, either in the dark or in the light. Protoporphyrin IX accumulations were estimated in dark-treated samples, using a simple methodology. In all cases, we have found a positive correlation between cellular damages and protoporphyrin IX accumulations. The results provide further evidences in favor of the light-dependent activity of…

0106 biological sciences0303 health sciencesProtoporphyrin IXChemistryHealth Toxicology and Mutagenesis[SDV]Life Sciences [q-bio]General MedicineMetabolismPyrazole01 natural sciencesPorphyrin[SDV] Life Sciences [q-bio]03 medical and health scienceschemistry.chemical_compoundTissue cultureBiochemistryProtoporphyrinGrowth inhibitionMode of actionAgronomy and Crop Science030304 developmental biology010606 plant biology & botany
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Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the correspondi…

1997

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 4…

0106 biological sciencesDNA ComplementaryMolecular Sequence DataBiology4-Hydroxyphenylpyruvate Dioxygenase01 natural sciencesBiochemistry03 medical and health sciencesDioxygenaseComplementary DNA[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biologyHomogentisate 12-dioxygenase0303 health sciencesBase SequenceSequence Homology Amino AcidMolecular massDioxygenase activityNucleic acid sequenceCell BiologyMolecular biologyDaucus carotaBiochemistryElectrophoresis Polyacrylamide Gel4-Hydroxyphenylpyruvate dioxygenaseResearch ArticleChromatography LiquidSubcellular Fractions010606 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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The Water to Water Cycles in Microalgae.

2016

In oxygenic photosynthesis, light produces ATP plus NADPH via linear electron transfer, i.e. the in-series activity of the two photosystems: PSI and PSII. This process, however, is thought not to be sufficient to provide enough ATP per NADPH for carbon assimilation in the Calvin-Benson-Bassham cycle. Thus, it is assumed that additional ATP can be generated by alternative electron pathways. These circuits produce an electrochemical proton gradient without NADPH synthesis, and, although they often represent a small proportion of the linear electron flow, they could have a huge importance in optimizing CO2 assimilation. In Viridiplantae, there is a consensus that alternative electron flow comp…

0106 biological sciences0301 basic medicineLightPhysiology[SDV]Life Sciences [q-bio]Cell RespirationMehler reactionPlastoquinonePlant ScienceWater to water cyclesPhotosynthesis01 natural sciences03 medical and health scienceschemistry.chemical_compoundWater CycleMicroalgaePhotosynthesisElectrochemical gradientPhotosystemOrganellesbiologyChemistryElectron transportRuBisCOfood and beveragesCell BiologyGeneral MedicineElectron transport chain030104 developmental biologybiology.proteinBiophysicsPhotorespirationOxidoreductases010606 plant biology & botanyPlantcell physiology
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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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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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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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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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Photoreceptors and respiratory electron flow involvement in the activity of acifluorfen-methyl and LS 82-556 on nonchlorophyllous soybean cells

1987

Abstract The diphenyl ether acifluorfen-methyl [AFM; methyl 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoate] and the pyridine derivative LS 82-556 [( S )-3- N -(methylbenzyl)carbamoyl-5-propionyl-2,6-lutidine] induce light-dependent polyunsaturated fatty acid peroxidation, leading to general membrane disruption. Although devoid of functional chloroplasts, cultured soybean cells are sensitive to AFM and LS 82-556 only in the light. The possible involvement of carotenoids and respiratory electron flow was examined by monitoring ethane evolution, fluorescein release, and dry weight/fresh weight ratio alteration. Herbicide effects on cells exposed to white light or blue light (380–540 n…

0106 biological sciencesStereochemistryHealth Toxicology and Mutagenesis[SDV]Life Sciences [q-bio]Antimycin ATRANSPORT D'ELECTRONS01 natural sciences03 medical and health scienceschemistry.chemical_compoundmedicineFluoresceinCarotenoidComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesTrifluoromethylDiphenyl etherGeneral MedicineChloroplast[SDV] Life Sciences [q-bio]MembraneMechanism of actionchemistryBiophysicsmedicine.symptomAgronomy and Crop Science010606 plant biology & botany
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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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Localization within chloroplasts of protoporphyrinogen oxidase, the target enzyme for diphenylether-like herbicides

1992

International audience

[SDV] Life Sciences [q-bio]MALHERBOLOGIE[SDV]Life Sciences [q-bio]ComputingMilieux_MISCELLANEOUS
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Mode of action of the herbicide siduron on wheat

1987

International audience

[SDV] Life Sciences [q-bio][SDV]Life Sciences [q-bio]ComputingMilieux_MISCELLANEOUS
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Protorphyrinogen oxidase inhibition by three peroxidizing herbicides : oxadiazon , LS 82-556 and M and B 39279

1989

International audience

SOLANUM TUBEROSUM MUS MUSCULUS[SDV.BC]Life Sciences [q-bio]/Cellular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUS
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Recent advances in the mode of action of diphenyl ethers and relates herbicides

1990

61 ref.; International audience

[SDV] Life Sciences [q-bio][SDV]Life Sciences [q-bio]
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Studies on the mode of action of acifluorfen-methyl in nonchlorophyllous soybean cells

1988

International audience

[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsComputingMilieux_MISCELLANEOUS
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Protorphyrinogen oxidase as a molecular target for diphenyl ether herbicides

1989

32 ref.; International audience

[SDV] Life Sciences [q-bio]SOLANUM TUBEROSUM MUS MUSCULUS[SDV]Life Sciences [q-bio]
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Characterization of the mode of action of the experimental herbicide LS 82-556 [ (S)3-N-(methylbenzyl) carbamyl-5-propionyl-2,6 lutidine

1986

34 ref.; International audience

[SDV] Life Sciences [q-bio][SDV]Life Sciences [q-bio]CORNICHON
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