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PubMed2005

Potential energy surfaces for gas-phase SN2 reactions involving nitriles and substituted nitriles.

The stationary points on the potential energy surfaces for a number of gas-phase S(N)2 reactions have been determined using a combination of pulsed ionization high-pressure mass spectrometry. MP2/6-311++G**//B3LYP/6-311+G** calculations are shown to provide excellent agreement with the experimentally determined values, providing confidence for the use of this computational method to predict values that are not available experimentally. The binding in the halide/nitrile complexes has been described in the past as either hydrogen bonding or electrostatic bonding. The trends in the binding energies observed here, though, cannot be rationalized in terms of simply hydrogen bonding or ion-dipole bonding but a mixture of the two. The computed structures support the description of binding as a mixture of hydrogen bonding and ion-dipole bonding.

Journal Article↗
PubMed2003

Nitrile hydrolysing activities of deep-sea and terrestrial mycolate actinomycetes.

Nitrile metabolising actinomycetes previously recovered from deep-sea sediments and terrestrial soils were investigated for their nitrile transforming properties. Metabolic profiling and activity assays confirmed that all strains catalysed the hydrolysis of nitriles by a nitrile hydratase/amidase system. Acetonitrile and benzonitrile, when used as growth substrates for enzyme induction experiments, had a significant influence on the biotransformation activities towards various nitriles and amides. The specific activities of selected deep-sea and terrestrial acetonitrile-grown bacteria against a suite of nitriles and amides were higher than those of the only other reported marine nitrile-hydrolysing R. erythropolis, isolated from a shallow sediment. The increase of nitrile chain length appeared to have negative influence on the nitrile hydratase activity of acetonitrile-grown bacteria, but the same was not true for benzonitrile-grown bacteria. The nitrile hydratases and amidases were constitutive in 10 of the 16 deep-sea and terrestrial actinomycetes studied, and one strain showed an inducible hydratase and a constitutive amidase. Most of the deep-sea strains had constitutive activities and showed some of the highest activities and broadest substrate specificities of organisms included in this study.

Acetamides↗
PubMed2005

Nocardia globerula NHB-2: a versatile nitrile-degrading organism.

A versatile nitrile-degrading bacterium was isolated by enrichment culture from the soil of a forest near Manali, Himachal Pradesh, India, and was identified as Nocardia globerula. This organism contains 3 enzymes with nitrile-degrading activity: nitrilase, nitrile hydratase, and amidase. Nocardia globerula NHB-2 cells grown on nutrient broth supplemented with 1% glucose and 0.1% yeast extract exhibited nitrile hydratase-amidase activity specific for saturated aliphatic nitriles or amide, while addition of acetonitrile in nutrient broth yielded cells with nitrile hydratase-amidase that in addition to saturated aliphatic nitriles-amide also hydrolyzed aromatic amide. Nocardia globerula NHB-2 cultivated on nutrient broth containing propionitrile exhibited nitrilase activity that hydrolyzed aromatic nitrile and unsaturated aliphatic nitrile. The versatility of this organism in the hydrolysis of various nitriles and amides makes it a potential bioresource for use in organic synthesis.

Amides↗
PubMed2005

Characterisation of the nitrile hydratase gene clusters of Rhodococcus erythropolis strains AJ270 and AJ300 and Microbacterium sp. AJ115 indicates horizontal gene transfer and reveals an insertion of IS1166.

The nitrile metabolising strains AJ270, AJ300 and AJ115 were isolated from the same location. The strains have very similar nitrile metabolising profiles. Sequencing of the 16S rRNA gene indicates that strains AJ270 and AJ300 are novel strains of Rhodococcus erythropolis while strain AJ115 is a novel Microbacterium strain very closely related to Microbacterium oxydans and Microbacterium liquefaciens. Analysis of the structure of the nitrile hydratase/amidase gene clusters in the three strains indicates that this region is identical in these strains and that this structure is different to other nitrile hydratase/amidase gene clusters. The major difference seen is the insertion of a complete copy of the insertion sequence IS1166 in the nhr2 gene. This copy of IS1166 generates a 10 bp direct duplication at the point of insertion and has one ORF encoding a protein of 434 amino acids, with 98% homology to the transposase of IS666 from Mycobacterium avium. A gene oxd, encoding aldoxime dehydratase is found upstream of the nitrile hydratase gene cluster and an open reading frame encoding a protein with homology to GlnQ type ABC transporters is found downstream of the nitrile hydratase/amidase genes. The identity of the nitrile hydratase/amidase gene clusters in the three strains suggests horizontal gene transfer of this region. Analysis of the strains for both linear and circular plasmids indicates that both are present in the strains but hybridisation studies indicate that the nitrile hydratase/amidase gene cluster is chromosomally located. The nitrile hydratase/amidase enzymes of strain AJ270 are inducible with acetonitrile or acetamide. Interestingly although a number of Fe-type nitrile hydratases have been shown to be photosensitive, the enzyme from strain AJ270 is not.

ATP-Binding Cassette Transporters↗
PubMed1996

Key role of alkanoic acids on the spectral properties, activity, and active-site stability of iron-containing nitrile hydratase from Brevibacterium R312.

Interaction of n-butyric acid with dialyzed nitrile hydratase from Brevibacterium R312, which is characterized by a charge-transfer band at 680 nm and EPR signals typical of a low-spin Fe(III) with delta g = 0.22, leads to a form displaying different spectral properties (lambda = 710 nm, delta g = 0.31). Butyric acid also acts as a competitive inhibitor of nitrile-hydratase-catalyzed hydration of acrylonitrile with a Ki value of 0.9 mM. Formation of the complex between the enzyme and butyric acid is highly dependent on the concentration of the latter and on pH. When stored with high levels of butyric acid, nitrile hydratase is completely inactive. The active uncomplexed enzyme is restored under the high dilution conditions used for the enzymatic assays, while the complexed form is favored at acidic pH and is not formed at pH above 8. Furthermore, the inhibitory potency of butyric acid decreases upon increasing pH (IC50 increases from 0.8 mM at pH 6.2 to 12 mM at pH 8.2). These data show that nitrile hydratase interacts with the acid form of butyric acid with a high affinity (Ki' approximately 4 microM at pH 7.2). At pH < 3, the visible spectrum of the enzyme disappears, presumably because of demetallation, whereas that of the complex exhibits a charge-transfer band shifted to 800 nm, the presence of butyric acid preventing nitrile hydratase from demetallation. Other linear carboxylic acids such as valeric and hexanoic acids behave similarly; they act as inhibitors of nitrile hydratase and protect the enzyme during storage. A structure of the nitrile hydratase active site interacting with butyric acid is tentatively proposed in which the latter is hydrogen-bonded to the Fe(III)-OH moiety. This interaction between butyric acid and nitrile hydratase should be considered when deducing the nature of nitrile hydratase active site and mechanisms, from spectral and enzymatic data, since most results published previously have been obtained on nitrile hydratase containing large amounts of butyric acid and interpreted without taking into account the presence of this acid in the active site.

Acrylonitrile↗
PubMed1990

Reversible covalent binding of peptide nitriles to papain.

The dissociation constants for reversible covalent binding of twelve peptide nitrile inhibitors to the active site of papain have been measured by means of fluorescence titration. The binding constants generally parallel the kinetic specificity constants (kcat/Km) for related papain substrates, supporting earlier suggestions that peptide nitriles behave as transition state analog inhibitors of papain. In ten cases the temperature dependence of binding was analyzed to determine the enthalpic and entropic contributions to the binding energy. A compensation plot of delta H vs. T delta S resulted in two parallel lines, one for 'specific' nitriles (i.e., N-Ac-L-aa-NHCH2CN; aa = Phe, Leu, Met) and the other for 'non-specific' nitriles (e.g., N-Ac-D-Phe-NHCH2CN, PhCH2CH2CONHCH2CN hippurylnitrile, etc.). For both specific and nonspecific nitriles representing an 1800-fold range of Kd values (0.27 microM-490 microM), the solvent deuterium isotope effect on binding (Kd(H2O)/Kd(D2O) = DKd) was very close to 2.0. This isotope effect could be accounted for entirely by the simple protonic change which occurs upon the reversible addition of the active site sulfhydryl of papain to the nitrile group of the peptide derivative to form a covalent thioimidate linkage. In contrast, six closely related non-nitrile ligands containing identical peptide side chains but having C-terminal groups incapable of binding covalently to papain had unmeasureably high dissociation constants. Collectively, these results indicate that strong binding of peptide nitrile substrate analogs to papain requires a combination of (1) hydrophobic interaction (especially at the P2 position), (2) specific intermolecular hydrogen bonding and (3) covalent interaction of the nitrile with the active site sulfhydryl group.

Chemical Phenomena↗
PubMed2001

Physiology, biochemistry and taxonomy of deep-sea nitrile metabolising Rhodococcus strains.

A collection of nitrile-hydrolysing rhodococci was isolated from sediments sampled from a range of deep coastal, and abyssal and hadal trench sites in the NW Pacific Ocean, as part of our programme on the diversity of marine actinomycetes. Nitrile-hydrolysing strains were obtained by batch enrichments on nitrile substrates with or without dispersion and differential centrifugation pre-treatment of sediments, and were recovered from all of the depths sampled (approximately 1100-6500 m). Two isolates obtained from the Ryukyu (5425 m) and Japan (6475 m) Trenches, and identified as strains of Rhodococcus erythropolis, were chosen for detailed study. Both of the deep-sea isolates grew at in situ temperature (4 degrees C), salinities (0-4% NaCl) and pressures (40-60 MPa), results that suggest, but do not prove, that they may be indigenous marine bacteria. However, the absence of culturable Thermoactinomyces points to little or no run off of terrestrial microbiota into these particular trench sediments. Nitrile-hydrolysis by these rhodococci was catalysed by a nitrile hydratase-amidase system. The hydratase accommodated aliphatic, aromatic and dinitrile substrates, and enabled growth to occur on a much wider range of nitriles than the only other reported marine nitrile-hydrolysing R. erythropolis which was isolated from coastal sediments. Also unlike the latter strain, the nitrile hydratases of the deep-sea rhodococci were constitutive. The possession of novel growth and enzyme activities on nitriles by these deep-sea R. erythropolis strains recommends their further development as industrial biocatalysts.

DNA, Ribosomal↗
PubMed2005

Comparing the level of dexterity offered by latex and nitrile SafeSkin gloves.

An increase in the occurrence of latex allergy has been concurrent with the increasing use of latex gloves by laboratory and healthcare workers. In recent years nitrile gloves have been used to replace latex gloves to prevent latex allergy. Nitrile gloves offer a comparable level of protection against chemical and biological agents and are more puncture resistant. However, if manual dexterity is compromised by nitrile gloves to a greater degree than latex then this may increase the risk of sharps injuries. The Purdue pegboard test, which measures both gross and fine finger dexterity, was used to test the dexterity levels of two glove types used at HPA CEPR; Kimberly-Clark SafeSkin nitrile and latex laboratory gloves. There was a statistically significant 8.6% increase in fine finger dexterity provided by latex compared with nitrile SafeSkin laboratory gloves but no difference in gross dexterity between the glove types. There was no significant relationship between glove dexterity and age or gender. The selection of glove size was influenced by the digit length of participants. Moreover, those with longer, thinner fingers appeared to have an advantage when using nitrile SafeSkin gloves. The level of dexterity provided by latex and nitrile SafeSkin gloves for tasks on a gross dexterity level are comparable and health workers will benefit from the non-allergenic properties of nitrile. For tasks requiring fine finger dexterity nitrile SafeSkin gloves may impede dexterity. Despite this, the degree of restriction appears to have a negligible impact on safety in this study when compared with the risk of latex sensitization and subsequent allergy. In addition to glove material, working practices must also take into account glove size, fit, grip and thickness, as these factors can all influence dexterity.

Adult↗
PubMedDate not supplied

Effect of dosing vehicle on the toxicity and metabolism of unsaturated aliphatic nitriles.

The effect of dosing vehicle on toxicity and metabolism of unsaturated aliphatic nitriles was investigated in male Sprague-Dawley rats. Five unsaturated aliphatic nitriles--acrylonitrile, methacrylonitrile, allylnitrile, crotononitrile and fumaronitrile--were prepared in five different dosing vehicles--saline, corn oil, safflower oil, mineral oil, olive oil and Tween-20. Groups of six male rats were given 0.5 LD50 doses of the nitriles by gavage and they were observed for 12 It for cholinomimetic and central nervous system effects. Cyanide and glutathione levels were determined in blood and various organs at 1, 3 and 6 h after nitrile administration and thiocyanate levels were determined at 6 h after nitrile administration. The results indicate that all the vehicles studied potentiated the toxicity of all the nitriles compared to nitriles administered in saline and significantly increased their metabolism to cyanide and thiocyanate and nitrile-induced depletion of glutathione in rats. This behavior of vehicles illustrates the difficulty of identifying suitable vehicles for administration of lipophilic compounds in toxicology studies.

Acrylonitrile↗
PubMed2000

Comparative developmental toxicities of aliphatic nitriles: in vivo and in vitro observations.

The effects on embryonic development of a series of eight saturated (acetonitrile, propionitrile, and n-butyronitrile) and unsaturated (acrylonitrile, methacrylonitrile, allylnitrile, cis-2-pentenenitrile, and 2-chloroacrylonitrile) nitriles were compared in vitro using the whole embryo culture system. Day 10 rat embryos were cultured for 46 h in rat serum in the presence of either of these chemicals. All the tested chemicals produced concentration-dependent decreases in growth and differentiation and increases in the incidences of morphologically abnormal embryos. A wide range of embryotoxic potency was observed, with 2-chloroacrylonitrile and acetonitrile at the extremes (lowest effect levels of 50 microM and 40 mM, respectively). No common pattern could be drawn for all the eight nitriles tested in vitro, although there were some similarities between the malformations elicited by propionitrile and n-butyronitrile or between those elicited by the five unsaturated nitriles. Presence of a rat hepatic microsomal fraction and NADPH in the culture medium enhanced the embryotoxic effects of the five unsaturated nitriles tested but had no effects on saturated nitriles embryotoxicity. In addition to these in vitro experiments, pregnant rats were given a single oral dose of each compound on Day 10 of gestation and the embryos were evaluated on Day 12 of gestation, i.e., at a time of development corresponding to the developmental stage at the end of the whole embryo culture. All the nitriles investigated produced the characteristic defects developed by embryos exposed to sodium cyanide in utero or in culture. Our results provide further evidence that maternal production of cyanide may contribute to the developmental toxicity of saturated and unsaturated nitriles and suggest that distinct metabolites derived from microsomal metabolism of unsaturated nitriles may also play a role.

Abnormalities, Drug-Induced↗