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[The mechanism of metabolic denitration of nitroheterocyclic compounds].

It has been found that denitration of nitroheterocyclic drugs (NHCC) in mouse liver homogenate is one of the pathways of their biotransformation. This process is accompanied by the release of NO and NO-heme iron complex formation. The yield of complex increases linearly with time of NHCC incubation with liver homogenate and depends on NHCC structure. The ESR spectrum of the complex represents a superposition of spectra of NO with hemoglobin and NO with the other heme-containing proteins. NHCC denitration is inhibited by metyrapone, which is an evidence of cytochrome P-450 involvement in their metabolic denitration.

Animals↗
PubMed1984

Synthesis and antihypertensive activity of 6,7-disubstituted trans-4-amino-3,4-dihydro-2,2-dimethyl-2H-1-benzopyran-3-ols.

A series of novel 6,7-disubstituted trans-3,4-dihydro-2, 2-dimethyl-4-pyrrolidino-(or piperidino)-2H-1-benzopyran-3-ols was prepared and tested for antihypertensive activity in the conscious spontaneously hypertensive rat (SHR) and compared with certain of their monosubstituted analogues. The potent blood pressure lowering activity of the 6-monosubstituted compounds was enhanced by incorporation of an acetylamino or amino group at C(7) and that of the 7-nitro-substituted compound by incorporation of an amino (but not an acetylamino group) at C(6). The combination of 6-nitro or 6-cyano with 7-(acetylamino) or 7-amino groups and 6-amino with 7-nitro groups in trans-4-pyrrolidino- or -4-piperidino-2,2-dimethyl-2H-1-benzopyranols conferred superior antihypertensive activity to hydralazine and to the calcium antagonist, nifedipine, in SHR. The synthetic route to these compounds involves the conversion of 2H-1-benzopyrans to bromohydrins that were treated with pyrrolidine or piperidine. Preparation of the 6-cyano-7-amino analogue was accomplished when 6-cyano-7-[(trifluoroacetyl)amino]-2,2-dimethylbenzopyran was used as starting material.

Animals↗
PubMed1989

High-performance liquid chromatographic separation of ring-oxidized metabolites of nitro-polycyclic aromatic hydrocarbons.

Nitro-polycyclic aromatic hydrocarbons (nitro-PAHs) are widespread genotoxic environmental pollutants, which require metabolic activation to exert their biological activities. Metabolism of nitro-PAHs generates ring-oxidized metabolites including epoxides, phenols, dihydrodiols and tetrahydrotetrols. Separation of the oxidized metabolites and related compounds of a series of isomeric nitro compounds derived from anthracene, benz[a]anthracene, benzo[a]pyrene and benzo[e]pyrene was studied by high-performance liquid chromatography (HPLC) of different types of columns (monomeric and polymeric; reversed-phase and normal-phase). In the reversed-phase HPLC system, the general elution order of these compounds is: parent nitro-PAHs greater than phenolic derivatives greater than epoxides greater than dihydrodiols greater than tetrahydrotetrols. Among the geometric isomers, trans-dihydrodiols with both hydroxyl groups at the quasiaxial positions were eluted earlier than those with the hydroxyl groups at the quasiequatorial positions. Orientation of the nitro substituent has also been found to be an important structural feature for determining the relative retention order. Among the geometric isomers of nitro-PAHs and trans-dihydrodiols, the isomers with their nitro groups perpendicular or nearly perpendicular to the aromatic rings were eluted faster than the analogues with their nitro groups parallel or nearly parallel to the aromatic rings. Normal-phase HPLC gave opposite retention order, but with different separability among some of the compounds. Therefore, combination of both reversed- and normal-phase HPLC provides efficient separation of the ring-oxidized derivatives of nitro-PAHs. Results are also presented to compare the separation efficiency among different types of columns used. The results suggest that the polarity of solutes is the principal factor for determining their HPLC retention time.

Chemical Phenomena↗
PubMed1985

Relationship between mutagenic potency in Salmonella typhimurium and chemical structure of amino- and nitro-substituted biphenyls.

All positional isomers of mononitro- and monoaminobiphenyls and those of dinitro-, diamino- and aminonitrobiphenyls, which have one substituent on each benzene ring, were assayed for mutagenicity in Salmonella typhimurium by the Ames method. The results suggest that the structural requirements favoring mutagenic activity are the presence of substituents at the 4-position and their absence at the 2'-position. The introduction of an amino group to the 3'- or 4'-position of 4-nitrobiphenyl or a nitro group to 3'- or 4'-position of 4-aminobiphenyl enhanced the mutagenicity. Among the mutagenic compounds, 4-nitro analogues were mutagenic in strains TA98 and TA100 in the absence of a microsomal metabolic activation system. Strain TA98NR was not reverted by the direct-acting mutagens, whereas strain TA98/1,8-DNP6 was as revertible as strain TA98; these results suggest that the direct-acting mutagenicity involves the reduction of the nitro group by bacterial nitroreductase but does not involve specific esterification enzymes.

Biphenyl Compounds↗
PubMed2005

Characterization of the in vitro metabolism of selective androgen receptor modulator using human, rat, and dog liver enzyme preparations.

Compound S4 [S-3-(4-acetylamino-phenoxy)-2-hydroxy-2-methyl-N-(4-nitro-3-trifluoromethyl-phenyl)-propionamide] is a novel nonsteroidal selective androgen receptor modulator that demonstrates tissue-selective androgenic and anabolic effects. The purpose of this in vitro study was to identify the phase I metabolites, potential species differences in metabolism, and the cytochromes P450 (P450s) involved in the phase I metabolism of S4 using 14C-S4, recombinant P450s, and other liver enzyme preparations from human, rat, and dog. The major phase I metabolism pathways of S4 in humans were identified as deacetylation of the B-ring acetamide group, hydrolysis of the amide bond, reduction of the A-ring nitro group, and oxidation of the aromatic rings, with deacetylation being the predominant pathway observed with most of the enzyme preparations tested. Among the major human P450 enzymes tested, CYP3A4 appeared to be one of the major phase I enzymes that could be responsible for the phase I metabolism of S4 [Km = 16.1 microM, Vmax = 1.6 pmol/(pmol x min)] in humans and mainly catalyzed the deacetylation, hydrolysis, and oxidation of S4. In humans, the cytosolic enzymes mainly catalyzed the hydrolysis reaction, whereas the microsomal enzymes primarily catalyzed the deacetylation reactions. Similar phase I metabolic profiles were observed in rats and dogs as well, except that the amide bond hydrolysis seemed to occur more rapidly in rats. In summary, these results showed that the major phase I reaction of S4 in human, rat, and dog is acetamide group deacetylation.

Amides↗
PubMed1975

Penicillinamidohydrolase in Escherichia coli. I. Substrate specificity.

Substrate specificity of the bacterial penicillinamidohydrolase (penicillinacylase, EC 3.5.1.11) from Escherichia coli was determined by measuring initial rates of enzyme hydrolysis of different substrates within zero order kinetics. Some N-phenylacetyl derivatives of amino acids and amides of phenylacetic acid and phenoxyacetic acid of different substituted amides of these acids or amides, structurally and chemically similar to these compounds, served as substrates. Significant differences in ratios of initial rates of the enzyme hydrolysis of different substrates were found using a toluenized suspension of bacterial cells or a crude enzyme preparation, in spite of the fact that the enzyme is localized between the cell wall and cytoplasmic membrane, in the so-called periplasmic space. N-phenylacetyl derivatives are the most rapidly hydrolyzed substrates. Beta-phenylpropionamide and 4-phenylbutyramide were not utilized as substrates. The substrate specificity of the enzyme is discussed with respect to a possible use of certain colourless compounds as substrates, hydrolysis of which yields chromophor products suitable for a simple and rapid assay of the enzyme activity.

Amides↗
PubMed1980

Properties of a complex of Fe(III)-soybean lipoxygenase-1 and 4-nitrocatechol.

Fe(III)-soybean lipoxygenase-1 yields with 4-nitrocatechol a green coloured 1 : 1 complex, which shows at pH 7.0 absorption maxima at 385 nm and 650 nm. The formation of this complex is reversible. The circular dichroism spectrum of the complex of Fe(III)-lipoxygenase-1 and 4-nitrocatechol has a positive band at around 380 nm and a negative band at around 450 nm and is significantly different from that of the Fe(III)-enzyme as such. 4-Nitrocatechol can be displaced from the green complex by 13-L-hydroperoxy-cis-9, trans-11-octadecadienoic acid, resulting in the formation of the blue complex between the Fe(III)-enzyme and 13-L-hydroperoxy-cis-9,trans-11-octadecadienoic acid both under aerobic and anaerobic conditions. Also linoleic acid competes with 4-nitrocatechol for the binding site on the Fe(III)-enzyme, as can be demonstrated under anaerobic conditions, ultimately leading to reduction of the Fe(III)-enzyme. The oxygenation of linoleic acid by Fe(III)-lipoxygenase-1 is inhibited by 4-nitrocatechol. From steady-state kinetics a non-competitive inhibition pattern is obtained. Probably it has to be considered as pseudo non-competitive because of the slow establishment of the complex equilibrium. An inhibition constant (K4NC) of 16.3 microM is found. On prolonged incubation of Fe(III)-lipoxygenase-1 and 4-nitrocatechol the green complex converts into a brown species. This conversion is found to be coupled with a change in the nature of the inhibition from reversible to irreversible. A complex between native lipoxygenase-1 and 4-nitrocatechol is found to be unlikely.

Catechols↗
PubMed1977

Occurrence of tryptophan in the enzymically active site of diphtheria toxin fragment A.

Tryptophan residues of diphtheria toxin fragment A have been modified by 2-hydroxy-5-nitrobenzyl bromide. Fragment A loses its ability to inactivate ADP-ribosylation of the elongation factor 2, as a function of the number of residues modified. Modification of one tryptophan residue provides a dramatic loss of enzymic activity suggesting the presence of one essential residue of this type in fragment A. Examination of fingerprint maps of chymotryptic peptides of fragment A after reaction with 2-hydroxy-5-nitrobenzyl bromide allows us to identify this tryptophan residue at position 153 of the amino acid sequence. ORD and CD experiments joined to immunochemical studies seem to exclude the possibility that the observed decrease in the enzymic activity may be attributed to a conformational change. Finally, results of nicotinamide-adenine dinucleotide-binding measurements suggest that tryptophan 153 would be concerned with the elongation factor 2 binding site or with the catalytic site itself.

Benzyl Compounds↗
PubMed2005

The assessment of the energetic compound 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-Hexaazaisowurtzitane (CL-20) degradability in soil.

CL-20 is a relatively new energetic compound with applications in explosive and propellant formulations. Currently, information about the fate of CL-20 in ecological systems is scarce. The aim of this study is to evaluate the biodegradability of CL-20 in soil environments. Four soils were used where initial CL-20 concentrations (above water solubility) ranged from 125 to 1500 mg of CL-20 per kg dry soil (corresponding to the concentrations derived from unexploded ordnance, low order detonation, or manufacturing spills). CL-20 appears to be biodegradable in soil under anaerobic conditions, and additions of organic substrates can substantially accelerate this process. However, CL-20 is not degraded in soil under aerobic conditions kept in the dark at temperatures up to 30 degrees C without organic amendments. Additions of starch or cellulose promote the biodegradation of CL-20 under aerobic conditions. Soil microbial community mediated biodegradation and plant uptake appears to enhance CL-20 biodegradation, the latter suggesting a possible route for CL-20 to entry in the food chain.

Aerobiosis↗
PubMed2005

Spectro-thermal decomposition study of 1,4-dinitroglycoluril (DINGU).

Simultaneous thermal analysis and high temperature FTIR study of 1,4-dinitroglycoluril (DINGU) is reported. TG showed 90% weight loss in the temperature range 225-250 degrees C. Isothermal TG of DINGU showed about 70% weight loss in the temperature range 210-230 degrees C. Kinetic parameters evaluated using a computer program showed that alpha-t data are best described by the Avrami-Erofeev's equation for n=2 with an activation energy of 165 kJ/mol. The kinetics of decomposition of DINGU was followed by studying NH (3388 cm(-1)), CO (1770-1810 cm(-1)) and NO2 symmetric stretching (1565-1570 cm(-1)) IR bands. All three bands showed loss of intensity with temperature and time. alpha-t data of decomposition with respect to NO2 stretching was again best described by the Avrami-Erofeev's equation for n=2. Gaseous decomposition products observed in the IR were N2O, NO2, CO2, HCN and NO. PM3 and Hartree-Fock level calculations on various bond lengths, bond angles and dihedral angles were computed to support the analysis of decomposition study using TG and IR. The data showed that CN and NH bonds are much shorter than the NN bonds, indicative of the weaker NN bond and hence, the possibilities of rupture of the same bond preferentially. This paper also discusses the sensitivity and performance properties of DINGU.

Explosions↗