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PubMed1999

The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site.

The periplasmic nitrate reductase, NapA, from Escherichia coli was identified as a 90 kDa molybdoprotein which comigrated during polyacrylamide gel electrophoresis with the di-haem c-type cytochrome, NapB. The DNA sequence of the 5' end of the napA gene and the N-terminal amino acid sequences of both NapA and NapB were determined. The 36 residue leader peptide for NapA includes the double-arginine motif typical of proteins to which complex redox cofactors are attached in the cytoplasm prior to targeting to the periplasm. The pre-NapA leader sequence is both unexpectedly long and, unless two successive proteolysis steps are involved, is cleaved at the unprecedented sequence G-Q-Q-. Nap activity was suppressed during growth in the presence of tungstate and was absent from a mutant unable to synthesise the molybdopterin cofactor.

Amino Acid Sequence↗
PubMed2000

Novel growth characteristics and high rates of nitrate reduction of an Escherichia coli strain, LCB2048, that expresses only a periplasmic nitrate reductase.

Escherichia coli strain LCB2048 is a double mutant defective in the synthesis of the two membrane-associated nitrate reductases A and Z. This strain can grow anaerobically on a non-fermentable carbon source, glycerol, in the presence of nitrate even in media supplemented with high concentrations of tungstate. This growth was totally dependent upon a highly active, periplasmic nitrate reductase (Nap). Due to the presence of a previously unreported narL mutation, synthesis of the periplasmic nitrate reductase by this strain was induced during anaerobic growth by nitrate. We have also demonstrated that methyl viologen is an ineffective electron donor to Nap: its use leads to an underestimation of the contribution of Nap activity to the rate of nitrate reduction in vivo.

Anaerobiosis↗
PubMed1983

Patch testing with sodium tungstate.

Hard metal contains about 90% tungsten carbide. In an investigation of the skin of 853 individuals who are still working or had previously worker in hard metal manufacture, sodium tungstate was included in a patch test with a panel of substances from the environment of the employees. No allergic reactions to tungstate were found. However, irritant pustular reactions appeared in 2.0% of the patch tests. The pustular reactions were often reproducible.

Dermatitis, Contact↗
PubMed1997

In vitro toxicity of cobalt and hard metal dust in rat and human type II pneumocytes.

It has been demonstrated that hard metal dust, which consists of a mixture of cobalt and tungsten carbide, is more toxic toward mouse peritoneal and rat alveolar macrophages than pure cobalt (Co) or tungsten carbide (WC). The aim of this study was to investigate the toxic effects of Co and hard metal dust on alveolar epithelial type II cells (AT-II), and to compare these with alveolar macrophages. Freshly isolated rat and human AT-II and rat alveolar macrophages were exposed for 18 hr to particles of Co, WC or Co/WC. As an index for cell toxicity, release of lactate dehydrogenase was measured. For rat AT-II, TD50 values per 10(5) cells were 672 micrograms (95% C.I. = 264-1706 micrograms) for pure Co and 101 micrograms (95% C.I. = 59-172 micrograms) for Co in Co/WC mixture. For rat alveolar macrophages, TD50 values per 10(5) cells were 18 micrograms (95% C.I. = 15-24 micrograms) for pure Co and 5 micrograms (95% C.I. = 5-6 micrograms) for Co in Co/WC mixture. WC only caused an increase in lactate dehydrogenase at high concentrations. No toxicity was found in human AT-II for either Co, WC or Co/WC. These results indicate that 1) rat AT-II are less sensitive to Co than rat alveolar macrophages, 2) human AT are less sensitive to Co than rat AT-II, 3) the toxicity of Co is increased by the presence of WC.

Animals↗
PubMed1994

Mineralized deposits in pulps of incompletely developed permanent monkey incisors after pulpotomy with tungsten carbide fissure burs.

The exposed pulp of incompletely developed permanent incisors of nine monkeys were treated with partial pulpotomy with tungsten carbide fissure burs on an air turbine equipment. The pulps were capped with calcium hydroxide (Dycal) followed by insertion of conventional amalgam. The results were studied by conventional light microscopy after 1 and 6 months. Rod-like mineralized pulpal deposits were seen in five of the nine animals, in 9 out of 67 teeth, evenly distributed at the two observation times. Also the lengths of the deposits appeared similar, while the thickness had increased markedly after 6 months. After 1 month the presence of a central vessel lumen was observed in the deposits. The results seemed to indicate that the mechanism of formation was an initial pathologic mineralization of the vessel wall, and a growth of the deposits by the elaboration of fibrous, atubular dentin on to the outside of this wall.

Animals↗
PubMed1990

An electron microscopic evaluation of the enamel surface subsequent to various debonding procedures.

In this study, enamel surface roughness was investigated following the use of various combinations of bonding agents, burrs and polishing procedures. Orthodontic brackets were bonded to 135 premolar teeth extracted from adolescents. Subsequent to debonding and finishing, the enamel surface was gold coated and examined in the scanning electron microscope. Each 200x photomicrograph was graded according to surface roughness and assigned to one of four selected standard grades. The use of different composites and different burs showed no significant effect on the finish of the enamel surface using Chi-square tests. Only two finishing procedures had a significant effect on surface roughness. The use of a Soflex disc followed by pumice slurry resulted in the roughest enamel surface and the use of pumice alone produced the smoothest enamel surface.

Adolescent↗
PubMed1992

Finishing techniques for amalgam restorations: clinical assessment at three years.

Use of the optimum finishing technique for an amalgam restoration may enhance the marginal integrity of the restoration and discourage its unnecessary early replacement. Two hundred and twenty-eight high copper amalgam restorations in 56 patients were evaluated, using clinical assessment criteria, up to three years after placement. Each patient had received at least one carved-only amalgam, at least one immediately finished restoration, and at least one amalgam that was polished at a subsequent appointment. Regardless of the finishing technique, the restorations exhibited similar marginal integrity up to three years after placement. Polished restorations were found to have substantially superior surface texture and less likelihood of surface discoloration. No evidence was found to support the use of immediate finishing techniques. The clinical significance of these findings, with respect to the need to polish amalgam restorations, is discussed.

Color↗
PubMed1997

Structure-based analysis of catalysis and substrate definition in the HIT protein family.

The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.

Acid Anhydride Hydrolases↗
PubMed1986

Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions.

Studies of polyanions that suppress scrapie have been done to pinpoint the cell types in the lymphoreticular system which are important in pathogenesis and to suggest possible prophylactic or therapeutic strategies for the unconventional slow viruses. A regime of three daily injections of the inorganic heteropolyanion HPA-23 reduced the effective scrapie dose by more than 99%; i.e., some mice survived peripherally injected doses of 100 50% lethal dose units. The effect was greatest when the first dose of HPA-23 was given 4 h after injecting scrapie, but it declined rapidly as this interval was increased, and there was virtually no effect 2 days after infection. A single dose of high-molecular-weight organic polyanions such as carrageenan or dextran sulfate (DS-500) greatly reduced (i.e., greater than 99%) the efficiency of scrapie infection. In contrast to HPA-23, DS-500 was equally effective whether given 4 days before or 8 h after the time of infection. The antiscrapie effect of DS-500 appeared to be independent of its activity as a B-cell mitogen and of its ability to produce a cytotoxic blockade of phagocytic cells. DS-500 probably caused the aggregation and loss from blood of scrapie inoculum which was present immediately after injection, but it had additional effects on scrapie at later times.

Animals↗
PubMed1988

Clinical trial of tolerance of HPA-23 in patients with acquired immune deficiency syndrome.

An open-label, multicenter clinical trial assessed the tolerance of HPA-23 (ammonium-21-tungsto-9-antimoniate) in patients with acquired immune deficiency syndrome. Sixty-nine patients were sequentially assigned to receive 0.25, 0.5, 1.0, or 2.0 mg of HPA-23 per kg intravenously 5 days per week for 8 weeks. HPA-23 was fairly well tolerated at doses of 1.0 mg/kg or less; nearly 60% of patients given 2.0 mg/kg discontinued treatment. Twenty-six patients discontinued treatment because of adverse events or concurrent illness. HPA-23 produced dose-related decreases in platelet count and increases in serum glutamine oxalacetic transaminase. There were no changes in immune system function, as determined by total lymphocyte count, T4-cell count, T8-cell count, and T4/T8 ratio. The effects of HPA-23 seemed to be more closely related to the total dose than to the daily dose. No improvement in the clinical status of the patients was observed during the 8 weeks of treatment.

Acquired Immunodeficiency Syndrome↗
PubMed1999

Sulfonates as terminal electron acceptors for growth of sulfite-reducing bacteria (Desulfitobacterium spp.) and sulfate-reducing bacteria: effects of inhibitors of sulfidogenesis.

This study demonstrates the ability of Desulfitobacterium spp. to utilize aliphatic sulfonates as terminal electron acceptors (TEA) for growth. Isethionate (2-hydroxyethanesulfonate) reduction by Desulfitobacterium hafniense resulted in acetate as well as sulfide accumulation in accordance with the expectation that the carbon portion of isethionate was oxidized to acetate and the sulfur was reduced to sulfide. The presence of a polypeptide, approximately 97 kDa, was evident in isethionate-grown cells of Desulfitobacterium hafniense, Desulfitobacterium sp. strain PCE 1, and the two sulfate-reducing bacteria (SRB)-Desulfovibrio desulfuricans IC1 (T. J. Lie, J. R. Leadbetter, and E. R. Leadbetter, Geomicrobiol. J. 15:135-149, 1998) and Desulfomicrobium norvegicum; this polypeptide was not detected when these bacteria were grown on TEA other than isethionate, suggesting involvement in its metabolism. The sulfate analogs molybdate and tungstate, effective in inhibiting sulfate reduction by SRB, were examined for their effects on sulfonate reduction. Molybdate effectively inhibited sulfonate reduction by strain IC1 and selectively inhibited isethionate (but not cysteate) reduction by Desulfitobacterium dehalogenans and Desulfitobacterium sp. strain PCE 1. Desulfitobacterium hafniense, however, grew with both isethionate and cysteate in the presence of molybdate. In contrast, tungstate only partially inhibited sulfonate reduction by both SRB and Desulfitobacterium spp. Similarly, another inhibitor of sulfate reduction, 1,8-dihydroxyanthraquinone, effectively inhibited sulfate reduction by SRB but only partially inhibited sulfonate reduction by both SRB and Desulfitobacterium hafniense.

Adenosine Triphosphate↗
PubMed2006

Genetic and biochemical evidence for the involvement of a molybdenum-dependent enzyme in one of the selenite reduction pathways of Rhodobacter sphaeroides f. sp. denitrificans IL106.

Selenite reduction in Rhodobacter sphaeroides f. sp. denitrificans was observed under photosynthetic conditions, following a 100-h lag period. This adaptation period was suppressed if the medium was inoculated with a culture previously grown in the presence of selenite, suggesting that selenite reduction involves an inducible enzymatic pathway. A transposon library was screened to isolate mutants affected in selenite reduction. Of the eight mutants isolated, two were affected in molybdenum cofactor synthesis. These moaA and mogA mutants showed an increased duration of the lag phase and a decreased rate of selenite reduction. When grown in the presence of tungstate, a well-known molybdenum-dependent enzyme (molybdoenzyme) inhibitor, the wild-type strain displayed the same phenotype. The addition of tungstate in the medium or the inactivation of the molybdocofactor synthesis induced a decrease of 40% in the rate of selenite reduction. These results suggest that several pathways are involved and that one of them involves a molybdoenzyme. Although addition of nitrate or dimethyl sulfoxide (DMSO) to the medium increased the selenite reduction activity of the culture, neither the periplasmic nitrate reductase NAP nor the DMSO reductase is the implicated molybdoenzyme, since the napA and dmsA mutants, with expression of nitrate reductase and DMSO reductase, respectively, eliminated, were not affected by selenite reduction. A role for the biotine sulfoxide reductase, another characterized molybdoenzyme, is unlikely, since its overexpression in a defective strain did not restore the selenite reduction activity.

Coenzymes↗
PubMed2006

Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters.

A novel tungstate and molybdate binding protein has been discovered from the hyperthermophilic archaeon Pyrococcus furiosus. This tungstate transport protein A (WtpA) is part of a new ABC transporter system selective for tungstate and molybdate. WtpA has very low sequence similarity with the earlier-characterized transport proteins ModA for molybdate and TupA for tungstate. Its structural gene is present in the genome of numerous archaea and some bacteria. The identification of this new tungstate and molybdate binding protein clarifies the mechanism of tungstate and molybdate transport in organisms that lack the known uptake systems associated with the ModA and TupA proteins, like many archaea. The periplasmic protein of this ABC transporter, WtpA (PF0080), was cloned and expressed in Escherichia coli. Using isothermal titration calorimetry, WtpA was observed to bind tungstate (dissociation constant [K(D)] of 17 +/- 7 pM) and molybdate (K(D) of 11 +/- 5 nM) with a stoichiometry of 1.0 mol oxoanion per mole of protein. These low K(D) values indicate that WtpA has a higher affinity for tungstate than do ModA and TupA and an affinity for molybdate similar to that of ModA. A displacement titration of molybdate-saturated WtpA with tungstate showed that the tungstate effectively replaced the molybdate in the binding site of the protein.

ATP-Binding Cassette Transporters↗
PubMed1982

Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli.

The bisC gene of Escherichia coli is tentatively identified as the structural gene for biotin sulfoxide reductase by the isolation of bisC(Ts) mutants that make thermolabile enzyme. The products of four other E. coli genes (chlA, chlB, chlE and chlG) are also needed for enzymatic activity. Mutations previously assigned to the bisA, bisB, and bisD genes belong to genes chlA, chlE, and chlG, respectively. The biotin sulfoxide reductase deficiency of a chlG, mutant is partially reversed by the addition of 10 mM molybdate to the growth medium. Mutational inactivation of the chlD gene reduces the specific activity of biotin sulfoxide reductase about twofold. This effect is reversed by the addition of 1 mM molybdate to the growth medium. The specific activity of biotin sulfoxide reductase is decreased about 30-fold by the presence of tungstate in the growth medium, an effect that has been observed previously with nitrate reductase and other molybdoenzymes. The specific activity of biotin sulfoxide reductase is not elevated in a lysate prepared by derepressing a lambda cI857 chlG prophage. Whereas biotin sulfoxide reductase prepared by sonic extraction of growing cells is almost completely dependent on the presence of a small heat-stable protein resembling thioredoxin, much of the enzyme obtained from lysates of thermoinduced lambda cI857 lysogens does not require this factor.

Acids↗