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PubMed1997

Medium-reductant directed expression of methyl coenzyme M reductase isoenzymes in Methanobacterium thermoautotrophicum (strain deltaH).

Methanobacterium thermoautotrophicum was grown in a chemostat under various controlled conditions in the presence of either sodium sulfide or sodium thiosulfate. After establishment of the steady state, cells were taken and examined for expression of the mRNA transcripts coding for the different forms of methyl coenzyme M reductase (MCR) and methylene tetrahydomethanopterin dehydrogenase (MDH). MCR isoenzyme II expression varied most markedly. Expression was found not only to depend on known parameters temperature, pH and gassing rate, but also on the medium composition, especially the reductant present.

Base Sequence↗

PubMed1996

Mutagenic activity of some coal-derived humic compounds evaluated by the Ames test.

Two coal-derived humic substances (Sulcis and South Africa, Eniricerche, Italy) have been evaluated for their mutagenic activity on TA98 and TA100 Salmonella typhimurium strains, either in presence or in absence of metabolic activation (S9). Both compounds showed no effect on the two strains, as observed with natural humic acid (Fluka). After chlorination, coal-derived humic acids induced a strong dose-related increase in the number of revertants on TA100 without S9, whose extent was directly proportional to the chlorination ratios. Such effect was completely suppressed when a sodium thiosulfate solution (10%) was added at the end of the chlorination period (about 90 h). The analogies with natural humic acid mutagenicity are discussed.

Antimutagenic Agents↗

PubMed1997

Comparison of five agents in protecting the cochlea against the ototoxic effects of cisplatin in the hamster.

The purpose of this investigation was to study the ameliorating effects of four agents on cisplatin-induced ototoxicity. Hamsters were given a series of five cisplatin injections either alone or in combination with sodium thiosulfate (STS), diethyldihydrothiocarbamate (DDTC), and S-2(3-aminopropylamino) ethylphosphorothioic acid (WR-2721), or fosfomycin. Ototoxicity was assessed anatomically by quantifying the extent of cochlear damage with the scanning electron microscope and physiologically with measures of the auditory brain stem response. When administered alone, cisplatin induced widespread loss of outer hair cells (OHCs) along much of the cochlea in the hamster, especially in the basal and middle turns, with an average survival of only 56% of the OHC population. In contrast, inner hair cells resisted cisplatin ototoxicity in the hamster. Thus the ameliorative effects of the different test agents were assessed by counting the number of surviving OHCs in each treatment group and comparing with cisplatin-treated controls. STS provided the most effective protection against the ototoxic effects of cisplatin, yielding 91% survival of OHCs. DDTC also reduced the ototoxic effects of cisplatin, yielding 68% survival of OHCs. Cotreatment with WR-2721 and fosfomycin yielded 45% and 52% OHC survival, respectively, and thus did not provide any chemoprotection. The results closely paralleled those based on auditory brain stem response recordings in that the magnitude of threshold shift was proportional to the amount of OHC loss; also, the amount of threshold shift at each frequency was in good agreement with the pattern of hair cell loss along the cochlear spiral. Thus both histologic and physiologic results suggest that STS and DDTC hold promise for ameliorating the ototoxic effects of cisplatin chemotherapy.

Amifostine↗

PubMed1998

Acute cyanide toxicity caused by apricot kernel ingestion.

A 41-year-old woman ingested apricot kernels purchased at a health food store and became weak and dyspneic within 20 minutes. The patient was comatose and hypothermic on presentation but responded promptly to antidotal therapy for cyanide poisoning. She was later treated with a continuous thiosulfate infusion for persistent metabolic acidosis. This is the first reported case of cyanide toxicity from apricot kernel ingestion in the United States since 1979.

Acidosis↗

PubMed2000

Distribution of rhodanese in different parts of the urogenital systems of sheep at pre- and post-natal stages.

The enzyme rhodanese (thiosulfate:cyanide sulfurtransferase) is a ubiquitous enzyme present in all living organisms, from bacteria to humans and plays a central role in cyanide detoxification. The purpose of this investigation is to determine and compare rhodanese activity in different parts of urogenital systems of male and female sheep fetuses at 2.5, 3, 3.5, 4, 4.5, and 5 months of age. The highest activity of rhodanese in male fetus was in kidney cortex, followed by medulla of the kidney. No significant difference was observed in other organs. In female fetus, the highest activity was in kidney cortex followed by oviduct and medulla of kidney. The enzyme activity of tissues increased with age. There was no significant difference (P > 0.05) between male and female fetuses in levels of rhodanese activity of different tissues except in urinary bladder at 2.5 and 3 months and in urethra at 4.5 months of age. The results of this study might indicate the involvement of rhodanese in cyanide detoxification in tissues which are more exposed to cyanide. On the other hand, rhodanese might perform other functions which are specific in these tissues.

Animals↗

PubMed2003

Distribution of rhodanese in tissues of goat (Capra hircus).

Rhodanese (thiosulfate: cyanide sulfurtransferase, EC. 2.8.1.1) is a ubiquitous enzyme present in all living organisms, from bacteria to humans and plays a central role in cyanide detoxification. The purpose of this investigation is to determine and compare rhodanese activity in different tissues of adult male and female goats (Capra hircus). The results showed that the specific activity of rhodanese in different tissues was significantly different (P<0.05). The highest activity of rhodanese was in epithelium of rumen, followed by epithelia of reticulum and omasum and liver. No significant difference was observed when tissues of male and female goats were compared. The lowest specific activity of rhodanese was observed in spleen, urinary bladder, lymph node, ovary, skeletal muscle and pyloric muscle of abomasum. The results of this study may indicate the involvement of rhodanese in cyanide detoxification in goat tissues that have greater potential to be exposed to higher levels of cyanide.

Animals↗

PubMed1998

Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese.

Mammalian rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) catalyzes the transfer of sulfane sulfur from donors such as S2O2-(3) and organic thiosulfonate anions (RS(O)2S-) to nucleophilic acceptors such as CN- and dithiols. The work reported here used an NADPH-coupled assay with thioredoxin reductase to show that reduced thioredoxin at micromolar concentrations is also an effective sulfur-acceptor substrate for rhodanese under conditions where millimolar concentrations of lipoate or dithiothreitol would be required. At near K(m) concentrations of the other substrate, apparent K(m) values for thioredoxin and methane thiosulfonate were 18.5 +/- 1.8 microM and 20 +/- 4 mM, respectively. The physiological compound alanine thiosulfonate also could serve as a donor substrate. In these systems, after a brief lag, inorganic sulfide accumulated as a final product. A formal mechanism in accord with all the results is proposed.

Animals↗

PubMed2000

Rhodanese as a thioredoxin oxidase.

A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been observed. Both isoforms were shown to be capable of using reduced thioredoxin as a sulfur-acceptor substrate. However, only the less negative form in common with the recombinant mammalian rhodanese expressed in E. coli, can also catalyze the direct oxidation of reduced thioredoxin evidently by reactive oxygen species. These activities are understood in terms of the established persulfide structure (R-S-SH) of the covalently substituted rhodanese in the sulfurtransferase reaction and an analogous sulfenic acid structure (R-S-OH) when the enzyme acts as a thioredoxin oxidase. The observations suggest a role for one rhodanese isoform in the detoxication of intramitochondrial oxygen free radicals.

Animals↗

PubMed1993

GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation.

Enzymatically active mammalian rhodanese, a mitochondrial matrix enzyme, which has been found to require assistants for efficient refolding in vitro, has been synthesized from a plasmid in a cell-free, fractionated, coupled transcription/translation system derived from Escherichia coli. The bacterial chaperonins, GroEL and GroES, along with the rhodanese substrate thiosulfate greatly enhance the specific enzymatic activity of the rhodanese polypeptide that is formed. Indirect evidence suggests that the effect of the GroEL/ES chaperonins is on ribosome-bound nascent peptides. The in vitro transcription/translation system produces sufficient amounts of rhodanese to provide a system for studying factors that control the initial steps in folding of nascent proteins.

Bacterial Proteins↗

PubMed1993

Physical characterization of a reactivatable liposome-bound rhodanese folding intermediate.

Recently, we described the formation of a complex between liposomes and the unfolded protein rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1), which could be liberated and efficiently reactivated after treatment of the complex with detergents [Zardeneta, G., & Horowitz, P. M. (1992) Eur. J. Biochem. 210, 831-837]. Previous data suggested that liposome-bound rhodanese was in the form of a folding intermediate. We have characterized in greater detail the nature of the conformation of the bound rhodanese. Physical characterization of the bound rhodanese intermediate was carried out using proteolysis, fluorescence studies with 1,8-anilinonapthalene-8-sulfonic acid, a probe for hydrophobic site exposure, intrinsic fluorescence to determine tryptophan accessibility using the quenchers acrylamide and iodide, and circular dichroism to detect extent of secondary structure. These studies show that the rhodanese intermediates bound to either cardiolipin or phosphatidylserine liposomes are not identical, the former being in a less compact conformation yet having more secondary structure than the latter, an observation which may explain why the reactivation of the former intermediate is more effective. Finally, turbidimetric and proteolytic studies raise the possibility that each rhodanese intermediate binds to several liposomes. This finding suggests that a possible reason for the differential reactivation yields obtained may be due to the fact that unfolded rhodanese has more binding sites for cardiolipin than for phosphatidylserine liposomes. A greater number of binding sites would result in better anchoring of rhodanese's interactive surfaces and thus reduce the likelihood of misfolding.

Anilino Naphthalenesulfonates↗

PubMed1985

Differential binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid to rhodanese catalytic intermediates.

Studies have been performed to quantitate the binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid (2,8-ANS) to catalytic intermediates of the enzyme rhodanese: the sulfur-substituted form (ES) and the sulfur-free form (E). The molecular 2,8-ANS has not been extensively used for protein studies, and some characterization is presented to demonstrate its usefulness as a probe for apolar binding sites. The molecule 2,8-ANS binds to at least two classes of sites on rhodanese. One class (class 1) is present in the ES form and has a Kd of 1.7 mM. The E form of rhodanese appears to have a second class of sites (class 2) in addition to the class 1 sites. Two independent fluorometric methods of analyzing the class 2 binding of 2,8-ANS to the E form gave an average value for Kd congruent to 179 microM. These fluorometric titrations, together with a Job plot, clearly indicate that 2,8-ANS binds to more than one site on the E form of rhodanese. The apparent apolarity is slightly higher for class 2 sites than for the class 1 sites, but both give Z factors of greater than 85. The substrate thiosulfate is able to displace the probe that is bound to the class 2 sites on the E form of the enzyme. Further, 2,8-ANS is found to be a competitive inhibitor of the catalyzed reaction with an apparent Kd of 170 microM. Circular dichroism measurements detect no significant changes in the average conformation of rhodanese that can be ascribed to the presence of 2,8-ANS.(ABSTRACT TRUNCATED AT 250 WORDS)

Anilino Naphthalenesulfonates↗

PubMed2003

Surface changes and role of buried water molecules during the sulfane sulfur transfer in rhodanese from Azotobacter vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study.

The Azotobacter vinelandii rhodanese is a sulfurtransferase enzyme that catalyzes the transfer of the outer sulfur atom from thiosulfate to cyanide. Recently, investigations by NMR relaxation on the (15)N-enriched protein reported that interdomain contacts are rigidly maintained upon the sulfane sulfur transfer from the enzyme to the substrate. The modality of the enzymatic mechanism is then confined to a surface interaction, including dynamics of water molecules buried in the tertiary structure. Thus, investigations have been carried out by fluorescence, circular dichroism, and nuclear magnetic relaxation dispersion measurements. The comparison of circular dichroism spectra of the persulfurated enzyme and the sulfur-free form indicated that small changes occur. Fluorescence quenching studies have been performed to evaluate the conformational changes during catalysis using the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid, and acrylamide, iodide, and cesium ions as quenchers. Changes in exchange dynamics of water molecules buried in the structure with bulk water, observed by nuclear magnetic relaxation dispersion, are due to local conformational transitions, likely involving residues around the active site, and are consistent with the global correlation time found by (15)N relaxation. These results, taken together, provide important information for elucidating the conformational features of the mechanism of action of the enzyme either in the role of a selective donor of a sulfur atom to small-sized substrates (i.e., to cyanide, transforming it into thiocyanate) or in the role of sulfur insertase for the formation of the Fe(2)S(2) iron-sulfur cluster in sulfur-deprived ferredoxins.

Azotobacter vinelandii↗

PubMed2005

Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.

The human MOCS3 protein contains an N-terminal domain similar to the Escherichia coli MoeB protein and a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 is proposed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin (MPT) synthase during Moco biosynthesis in humans. Recent studies have shown that the MOCS3 rhodanese-like domain (MOCS3-RLD) catalyzes the transfer of sulfur from thiosulfate to cyanide and is also able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z. MOCS3-RLD contains four cysteine residues of which only C412 in the six amino acid active loop is conserved in homologous proteins from other organisms. ESI-MS/MS studies gave direct evidence for the formation of a persulfide group that is exclusively formed on C412. Simultaneous mutagenesis of the remaining three cysteine residues showed that none of them is involved in the sulfur transfer reaction in vitro. A disulfide bridge was identified to be formed between C316 and C324, and possible roles of the three noncatalytic cysteine residues are discussed. By ESI-MS/MS a partially gluconoylated N-terminus of the His6-tagged MOCS3-RLD was identified (mass increment of 178 Da) which resulted in a heterogeneity of the protein but did not influence sulfurtransferase activity.

Amino Acid Sequence↗

PubMed2005

Recovery of chlorine-exposed Escherichia coli in estuarine microcosms.

Laboratory microcosm experiments were performed to determine whether chlorine-exposed Escherichia coli are capable of recovery (i.e., increase in numbers of culturable cells) in estuarine waters and if so what water-quality parameters are responsible for this recovery. Suspensions of E. coli were exposed to 0.5 mg L(-1) of chlorine for 5 min followed by dechlorination with sodium thiosulfate. The chlorine-exposed bacteria were introduced into 2-L microcosms containing estuarine water collected from the Seacoast region of New Hampshire. Culturable cells in the microcosms were enumerated at 0, 10, 24, 48, and 74 h. In all estuarine microcosms the number of culturable cells increased by factors ranging from 2.8 to 50 over the 74-h incubation period. Multiple linear regression analyses indicated that ammonium and salinity were most significantly correlated with the recovery of E. coli over the 74-h incubation period; however, ammonium concentrations were strongly correlated with dissolved organic carbon and total dissolved nitrogen, making it impossible to determine with any degree of certainty the unique effect nitrogen or carbon had on recovery. The extensive recovery observed in our study indicates that following exposure to concentrations of chlorine that cause cell injury rather than death, numbers of culturable E. coli may increase significantly when discharged into estuarine waters. Thus, depending on the effectiveness of the chlorination process, the regular monitoring of chlorinated wastewater treatment effluent may underestimate the true impact on water-quality and public health risks.

Antioxidants↗

PubMed2005

Analysis of atmospheric sesquiterpenes: sampling losses and mitigation of ozone interferences.

Atmospheric standards containing parts-per-billion levels of 14 semivolatile hydrocarbon compounds, including eight sesquiterpenes (SQTs) (longipinene, alpha-copaene, isolongifolene, alpha-cedrene, trans-caryophyllene, aromadendrene, alpha-humulene, delta-cadinene), two oxidized sesquiterpenoids (cisnerolidol, trans-nerolidol), one biogenic ketone (geranylacetone) and three aromatic compounds (1,3,5-triisopropylbenzene, diphenylmethane, nonylbenzene), were collected onto four solid adsorbent materials at increasing ozone mixing ratios (0-100 ppbv 03) for analysis by thermodesorption-gas chromatography. Substantial sampling losses of up to >90% were found for the most reactive SQT, even at the lowest ozone level investigated of 20 ppbv. Loss rates from the ozone-SQT reaction were used to derive estimates of gas-phase ozone reaction rate constants for longipinene, alpha-copaene, isolongifolene, geranylacetone, aromadendrene, delta-cadinene, cis-nerolidol, and transnerolidol. Three different ozone mitigation techniques were investigated to prevent these sampling losses. These strategies included (a) placing glass fiber filters impregnated with sodium thiosulfate (Na2S2O3) into the sampling line, (b) titration of ozone in the sampling stream with nitric oxide (NO), and (c) catalytically removing ozone with a commercially available manganese dioxide (MnO2) catalyst. All three techniques reduced ozone-mixing ratios from 100 ppbv to <0.6 ppbv at sampling flow rates of 1 L min(-1). When the Na2S2O3 filters and the NO-titration techniques were applied, SQT loss rates decreased from 25-60% to 0-5% for most SQT compounds and from >90% to approximately 10-50% for the two most reactive compounds at ozone mixing ratios of up to 100 ppbv. The commercial manganese dioxide scrubber, however, caused complete analyte losses (>98%) even at 0 ppbv ozone. These results underline the need and present applicable techniques for removal of ozone in air samples for SQT analysis by solid adsorption techniques.

Adsorption↗

PubMed2000

Adaptation of methane formation and enzyme contents during growth of Methanobacterium thermoautotrophicum (strain deltaH) in a fed-batch fermentor.

During growth of Methanobacterium thermoautotrophicum in a fed-batch fermentor, the cells are confronted with a steady decrease in the concentration of the hydrogen energy supply. In order to investigate how the organism responds to these changes, cells collected during different growth phases were examined for their methanogenic properties. Cellular levels of the various methanogenic isoenzymes and functionally equivalent enzymes were also determined. Cells were found to maintain the rates of methanogenesis by lowering their affinity for hydrogen: the apparent Km(H2) decreased in going from the exponential to the stationary phase. Simultaneously, the maximal specific methane production rate changed. Levels of H2-dependent methenyl-tetrahydromethanopterin dehydrogenase (H2-MDH) and methyl coenzyme M reductase isoenzyme II (MCR II) decreased upon entry of the stationary phase. Cells grown under conditions that favored MCR II expression had higher levels of MCR II and H2-MDH, whereas in cells grown under conditions favoring MCR I, levels of MCR II were much lower and the cells had an increased affinity for hydrogen throughout the growth cycle. The use of thiosulfate as a medium reductant was found to have a negative effect on levels of MCR II and H2-MDH. From these results it was concluded that M. thermoautotrophicum responds to variations in hydrogen availability and other environmental conditions (pH, growth temperature, medium reductant) by altering its physiology. The adaptation includes, among others, the differential expression of the MDH and MCR isoenzymes.

Adaptation, Physiological↗

PubMed2000

Contact allergy and hand eczema in Swedish dentists.

Hand eczema and contact allergy in Swedish dentists were studied in a multidisciplinary project. The aims of the study were to establish diagnoses, to investigate the occurrence of contact allergy, in particular to (meth)acrylates, and to evaluate certain consequences of hand eczema. A postal questionnaire on skin symptoms, atopy and occupational experience was mailed to 3,500 dentists aged <65 years, and licensed 1965-1995. The response rate was 88%. Among dentists living in 3 major cities, 14.9% (n= 191) reported hand eczema during the previous year. They were invited to a clinical examination, including patch testing with a standard and a dental series. 158/191 (83%) dentists attended, and hand eczema diagnosis was confirmed in 149/158 (94%). Irritant contact dermatitis was diagnosed in 67% and allergic contact dermatitis in 28%. On patch testing, 50% presented at least 1 positive reaction. The most frequent allergens were nickel sulfate, fragrance mix, gold sodium thiosulfate and thiuram mix. 7 (5%) had positive reactions to (meth)acrylates, all to 2-hydroxyethyl methacrylate and 6 also to ethyleneglycol dimethacrylate. 38% had consulted a physician, 4% had been on sick-leave and 1% had changed occupational tasks due to hand eczema. No dentist with allergy to acrylates had been on sick-leave or changed occupation. It is concluded that dentistry is a high-risk occupation for hand eczema, and that irritant contact dermatitis is most common. The prevalence of contact allergy to acrylates was below 1% in the population of responding dentists, and in most cases did not have serious medical, social or occupational consequences.

Adult↗

PubMed2001

Is contact allergy in man lifelong? An overview of patch test follow-ups.

In contradistinction from certain strains of mice, contact allergy in man is hypothesized to be either lifelong or at least to last for years. We examined follow-up studies on contact allergy, as evaluated by patch testing, attempting to quantify its natural history. The allergens include colophonium, gold sodium thiosulfate, nickel, and cobalt. At present, due to technical limitations, we cannot state in quantitative terms whether contact allergy in man is lifelong and whether its clinical manifestations change. Thus, we list some criteria for future studies which may help resolve the above question.

Antirheumatic Agents↗