Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Diuron”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 145 records · Page 8Linked to original sources
PubMed1983

Interaction of chloroplasts with inhibitors: effects of two diphenylether herbicides, fomesafen and nitrofluorfen, on electron transport, and some comparisons with dibromothymoquinone, diuron, and paraquat.

Several effects on pea (Pisum sativum L. var Onwards) chloroplasts of a new diphenylether herbicide, fomesafen (5-[2-chloro-4-trifluoromethyl-phenoxy]-N-methanesulfonyl-2 -nitrobenzamide) have been compared with those of a herbicide of related structure, nitrofluorfen (2-chloro-1-[4-nitrophenoxy]-4-[trifluoromethyl]benzene). Although both compounds produce the same light-dependent symptoms of desiccation and chlorosis indicative of a common primary mechanism of action, this study is concerned with a more broadly based investigation of different effects on the electron transport system. Comparisons have also been made with other compounds interacting with the chloroplast. Unlike nitrofluorfen, fomesafen has little effect as an inhibitor of electron flow or energy transfer. Both compounds have the ability to stimulate superoxide production through a functional electron transport system, and this involves specifically the p-nitro substituent. The stimulation, which is not likely to be an essential part of the primary herbicidal effect, is diminished under conditions that remove the coupling factor. Evidence suggests that both diphenylethers may be able to bind to the coupling factor, and kinetic studies reveal this for dibromothymoquinone as well. Such a binding site might be an important feature in allowing the primary effect of the diphenylether herbicides to be expressed.

Journal Article↗
PubMed2001

Evaluation of fish models of soluble epoxide hydrolase inhibition.

Substituted ureas and carbamates are mechanistic inhibitors of the soluble epoxide hydrolase (sEH). We screened a set of chemicals containing these functionalities in larval fathead minnow (Pimphales promelas) and embryo/larval golden medaka (Oryzias latipes) models to evaluate the utility of these systems for investigating sEH inhibition in vivo. Both fathead minnow and medaka sEHs were functionally similar to the tested mammalian orthologs (murine and human) with respect to substrate hydrolysis and inhibitor susceptibility. Low lethality was observed in either larval or embryonic fish exposed to diuron [N-(3,4-dichlorophenyl), N'-dimethyl urea], desmethyl diuron [N-(3,4-dichlorophenyl), N'-methyl urea], or siduron [N-(1-methylcyclohexyl), N'-phenyl urea]. Dose-dependent inhibition of sEH was a sublethal effect of substituted urea exposure with the potency of siduron < desmethyl diuron = diuron, differing from the observed in vitro sEH inhibition potency of siduron > desmethyl diuron > diuron. Further, siduron exposure synergized the toxicity of trans-stilbene oxide in fathead minnows. Medaka embryos exposed to diuron, desmethyl diuron, or siduron displayed dose-dependent delays in hatch, and elevated concentrations of diuron and desmethyl diuron produced developmental toxicity. The dose-dependent toxicity and in vivo sEH inhibition correlated, suggesting a potential, albeit undefined, relationship between these factors. Additionally, the observed inversion of in vitro to in vivo potency suggests that these fish models may provide tools for investigating the in vivo stability of in vitro inhibitors while screening for untoward effects.

Animals↗
PubMed1977

Mitochondrial heredity of resistance to 3-(3,4-dichlorophenyl)-1,1-dimethylurea, an inhibitor of cytochrome b oxidation, in Saccharomyces cerevisiae.

3-(3,4-dichlorophenyl)-1,1-dimethylurea (diuron), an inhibitor of cytochrome b oxidation, has been used for the selection of three resistant mutants (diur) of Saccharomyces cerevisiae. The mutant diur-64 exhibits in vivo cross-resistance to antimycin A while diur-34 and diur-1 are more sensitive to antimycin A than the parental strain. The three mutants exhibit mitochondrial inheritance according to the following criteria: mitotic segregation of diuron-resistant and diuron-sensitive diploids is obtained among the diploid progeny of a cross between diur and dius; non-Mendelian segregation of diuron resistance (4:0) is observed in spores of tetrads issued from diuron-resistant diploid; extensive ethidium bromide treatment leads to the formation of Q- mutants which no longer transmit diur and dius alleles. Evidence for two distinct diuron-resistant loci were obtained by allelism tests. Recombination analysis shows that diuron-resistance is not located in the polar region of the mitochondrial genome. The diur loci are not linked to the erythromycin locus since the upper limit in recombinants frequency (26%) for a non-polar region is obtained between diur and eryr. A low recombinants frequency (3%) is observed in crosses between diur-34 mutation and the two mutants cob1 and cob2 suggesting that diur-34 might be located between these two cytochrome-b-deficient loci. The resistance to diuron is also expressed in vitro since the oxidation rates of succinate by sonicated submitochondrial particles from the mutants are clearly less sensitive to diuron than that of the wild type.

Antimycin A↗
PubMed2006

Homogeneous indirect fluorescence quenching immunoassay for the determination of low molecular weight substances.

This paper describes the principle of a homogeneous indirect fluorescence quenching immunoassay that uses monoclonal antibodies. It is a carrier-free assay system that is performed completely in solution. The assay system was established for the determination of a low molecular weight substance (hapten), the herbicide diuron, used as a model analyte. A fluorescein-monuron conjugate together with a fluorescence-quenching monoclonal anti-fluorescein antibody and an anti-analyte antibody (here an anti-diuron/monuron monoclonal antibody) were used as central components of the assay. The fluorescein-monuron conjugate can be bound either by the anti-fluorescein monoclonal antibody or by the anti-diuron/monuron monoclonal antibody. Due to steric hindrance, binding of both antibodies to the conjugate was not possible at the same time. By selecting the antibody concentrations appropriately, a dynamic equilibrium can be established that permits the preferential binding of the anti-diuron/monuron antibody to the conjugate, which allows the fluorescein in the conjugate to fluoresce. This equilibrium can be easily altered by adding free analyte (diuron), which competes with the conjugate to bind to the anti-diuron/monuron antibody. A reduction of anti-diuron/monuron antibody binding to the conjugate results in an increase in the binding of the anti-fluorescein antibody, which leads to a decrease in the fluorescence of the conjugate. The fluorescence is therefore a direct indicator of the state of equilibrium of the system and thus also the presence of free unconjugated analyte. The determination of an analyte based on this test principle does not require any washing steps. After the test components are mixed, the dynamic equilibrium is rapidly reached and the results can be obtained in less than 5 min by measuring the fluorescence of the fluorescein. We used this test principle for the determination of diuron, which was demonstrated for concentrations of approximately 5 nM.

Antibodies, Monoclonal↗
PubMed2003

Pesticide adsorptivity of aged particulate matter arising from crop residue burns.

Particulates (ashes) arising from the burning of crop residues are potentially effective adsorbents for pesticides in agricultural soils. To determine the long-term adsorptive sustainability of ashes, a wheat (Triticum aestivum L.) ash was aged under environmentally relevant conditions (in CaCl(2) solution at room temperature and pH 7) in soil extract for 1 month and in a soil (1% ash) for a period of up to 12 months. The aged ash and ash-amended soil were used to sorb diuron from water. The diuron sorption was also measured in the presence of atrazine as a competing pesticide. There was no observed microbial impact on the stability of the wheat ash in soil. All isotherms with the ash were nonlinear type-I curves, suggestive of the surface adsorption. On a unit mass basis, the ash in soil extract was 600-10000 times more effective than the soil in sorbing diuron. Adsorption of dissolved soil organic matter (DOM) during aging on the ash surfaces reduced the diuron adsorption by 50-60%. Surface competition from the atrazine adsorption also reduced the ash adsorption of diuron by 10-30%. A total of 55-67% reduction in diuron sorption by the ash-amended soil was observed. Due to its high initial adsorptivity, the ash fraction of the aged ash-amended soil contributed >50% to the total diuron sorption. Thus, the wheat ash aged in the soil remained highly effective in adsorbing diuron. As crop residues are frequently burned in the field, pesticides in agricultural soils may be highly immobilized due to the presence of ashes.

Adsorption↗
PubMed1982

Degradation of selected phenylurea herbicides by anaerobic pond sediment.

Anaerobic degradation of diuron [3-(3,4-dichlorophenyl)-1,1-dimethylurea], monuron [3-(4-chlorophenyl)-1,1-dimethylurea], and fenuron [1,1-dimethyl-3-phenylurea] were studied. Herbicide containing media (reduced with cysteine-HCl and under 95% N2:5% CO2 gas phase) were inoculated with pond sediments. Sediment from a diuron-treated pond dehalongenated diuron to 3-(3-chlorophenyl)-1,1-dimethylurea (CPDU) in 17 to 25 days but sterile sediment from the pond did not. Sediments from non-diuron treated ponds were also ineffective. Particles from diuron-treated sediment were essential for dehalogenation and they could not be replaced with other solid surfaces such as clay, sand or cellulose. Diuron was degraded by sediment at 25 and 30 degrees C (maximal rate) but not at 5, 15 and 37 degrees C after 55 days incubation. The product CPDU produced in laboratory cultures was found in sediment of the diuron-treated pond, indicating in situ reductive dechlorination. Sediment-inoculated cultures containing monuron and fenuron showed no degradation after 74 days incubation.

Biodegradation, Environmental↗
PubMed1981

Modification of the spectral properties of cytochrome b in mutants of Saccharomyces cerevisiae resistant to 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Mapping at two distinct genetic loci of the split mitochondrial gene of cytochrome b.

The effects of five inhibitors of the cytochrome bc1 complex: 3-(3,4-dichlorophenyl)-1,1-dimethylurea (diuron), 2-n-heptyl-4-hydroxyquinoline-N-oxide (HpHOQnO), antimycin A, funiculosin and mucidin were measured in submitochondrial particles of strains of the yeast Saccharomyces cerevisiae belonging to two classes of diuron-resistant mutants Diu 1 and Diu 2 which are modified in different exons of the split mitochondrial gene of cytochrome b. 1. The oxidation of NADH and of cytochrome b-561 exhibits a similar resistance to diuron and HpHOQnO in Diu 1 and Diu 2 mutants. 2. No extra reduction of cytochrome b-561 and cytochrome b-565 is observed in the presence of diuron and HpHOQnO. 3. Both Diu 1 and Diu 2 mutants exhibit the red shift of cytochrome b-561 induced by concentrations of HpHOQno 2 -- 3-times higher than those required in the parental strains. 4. The spectral and respiratory effects of antimycin A, funiculosin and mucidin and generally similar in the diuron-resistant mutants and in their parental strains. However a cross-resistance between diuron and antimycin A is indicated in one Diu 2 mutant. 5. From the combined genetic and biochemical data it is concluded that the interaction of diuron and HpHOQnO with cytochrome b is mediated by at least two specific amino acids located apart in the central region of the apocytochrome b peptide coded by mitochondrial DNA. These two amino acids control tightly the extra reduction of cytochromes b-565 and b-561 as well as the flow of electrons through the bc1 complex. However the binding of HpHOQnO required for the expression of the red shift of cytochrome b-561 is only slightly affected by the diu-1 and diu-2 mutations.

Antimycin A↗
PubMed2005

Monitoring of antifouling booster biocides in water and sediment from the port of Osaka, Japan.

Concentrations of booster antifouling compounds in the port of Osaka, Japan were assessed. Concentrations of Sea-Nine 211 (4,5-dichloro-2-n-octyl-3-isothiazolone), thiabendazole (2-(4-thiazolyl)-benzimidazole), IPBC (3-iodo-2-propynyl butylcarbamate), Diuron (3,4-dichlorophenyl-N, N-dimethylurea), Irgarol 1051 (2-methylthio-4-t-butylamino-6-cyclopropylamino-s-triazine), and M1 (2-methylthio-4-t-butylamino-6-amino-s-triazine) in port water samples were in the range of <0.003-0.004 microg L(-1), <0.0008-0.020 microg L(-1), <0.0007-1.54 microg L(-1), <0.0008-0.267 microg L(-1), and <0.0019-0.167 microg L(-1), respectively. IPBC was not detected in the water samples, but the concentration of Diuron was higher than any previously reported. The concentrations of Sea-Nine 211, thiabendazole, Diuron, Irgarol 1051, and M1 in sediment samples were in the range of <0.04-2.4 microg kg(-1) dry, <0.08-1.2 microg kg(-1) dry, <0.64-1350 microg kg(-1) dry, <0.08-8.2 microg kg(-1) dry, and <0.18-2.9 microg kg(-1) dry, respectively. IPBC was again not detected. The levels of Sea-Nine 211, Diuron, and Irgarol 1051 in water and sediment samples were high in a poorly flushed mooring area for small and medium-hull vessels. Levels of Diuron and Irgarol 1051 were highest in summer. The concentration of Sea-Nine 211 in water increased between August and October 2002. Except for M1, increases in the levels of booster biocides in sediment were observed during the study period. The sediment-water partition (Kd) was calculated by dividing the concentrations in sediment by the concentrations in water. The Kd values for Sea-Nine 211, thiabendazole, Diuron, Irgarol 1051, and M1 were 690, 180, 2700, 300, and 870. The Kd value for these alternative compounds was lower than for TBT.

Antinematodal Agents↗