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PubMed2004

Growth kinetics of haloalkaliphilic, sulfur-oxidizing bacterium Thioalkalivibrio versutus strain ALJ 15 in continuous culture.

The chemolithoautotrophic, sulfur-oxidizing bacterium Thioalkalivibrio versutus strain ALJ 15, isolated from a soda lake in Kenya, was grown in a continuous culture, with thiosulfate or polysulfide as growth-limiting energy source and oxygen as electron acceptor, at pH 10 and at pH 0.6, 2 M and 4 M total sodium. The end product of the sulfur-compound oxidation was sulfate. Elemental sulfur and a cell-bound, polysulfide-like compound appeared as intermediates during substrate oxidation. In the thiosulfate-limited culture, the biomass yields and maximum specific growth rates decreased two and three times, respectively, with increasing sodium concentration. The apparent affinity constant measured for thiosulfate and polysulfide was in the micromolar range (Ks = 6 +/- 3 microM). The maintenance requirement (ms = 8 +/- 5 mmol S2O3(2)/g dry weight h(-1)) was in the range of values found for other autotrophic sulfur-oxidizing bacteria. The organism had a comparable maximum specific rate of oxygen uptake with thiosulfate, polysulfide, and sulfide, while elemental sulfur was oxidized at a lower rate. Glycine betaine was the main organic compatible solute. The respiration rates with different species of polysulfides (Sn2-) were tested. All polysulfide species were completely oxidized at high rates to sulfate. Overall data demonstrated efficient growth and sulfur compounds oxidation of haloalkaliphilic chemolithoautotrophic bacteria from soda lakes.

Biomass↗

PubMed1983

Reduction of bisulfite by the trithionate pathway by cell extracts from Desulfotomaculum nigrificans.

Bisulfite was reduced to sulfide by cell extracts of Desulfotomaculum nigrificans. When trithionate was added to reaction mixtures reducing bisulfite, sulfide formation was inhibited with accumulation of thiosulfate. The thiosulfate reductase activity of cell extracts was found to be inhibited by trithionate. Trithionate alone was reduced to thiosulfate and purified bisulfite reductase (P582) was not affected by trithionate. It is concluded that the pathway for bisulfite reduction in Dt. nigrificans includes trithionate and thiosulfate as intermediate compounds.

Gram-Negative Anaerobic Bacteria↗

PubMed1986

Stereospecific effect of naloxone hydrochloride on cyanide intoxication.

Cyanide intoxication in mice can be antagonized by the opiate antagonist, (-)naloxone HCl, alone or in combination with sodium thiosulfate and/or sodium nitrite. Potency ratios, derived from LD50 values, were compared in groups of mice pretreated with sodium nitrite (sc, 100 mg/kg), sodium thiosulfate (ip, 1 g/kg), and (-)naloxone HCl (sc, 10 mg/kg) either alone or in various combinations. These results indicate that naloxone HCl provides a significant protection against the lethal effects of potassium cyanide. The protective effect of sodium thiosulfate, but not sodium nitrite, was enhanced with (-)naloxone HCl. The combined administration of sodium nitrite and sodium thiosulfate was further enhanced with (-)naloxone HCl. This protective effect of naloxone HCl against the lethal effect of cyanide appears to be restricted to the (-)stereoisomer, as the (+)stereoisomer, the inactive opiate antagonist, is also inactive in protecting against the lethal effects of cyanide. The mechanism of antagonism is discussed.

Animals↗

PubMed1983

Interaction of rhodanese with mitochondrial NADH dehydrogenase.

NADH dehydrogenase is an iron-sulfur flavoprotein which is isolated and purified from Complex I (mitochondrial NADH: ubiquinone oxidoreductase) by resolution with NaClO4. The activity of the enzyme (followed as NADH: 2-methylnaphthoquinone oxidoreductase) increases linearly with protein concentration (in the range between 0.2 and 1.0 mg/ml) and decreases with aging upon incubation on ice. In the present work a good correlation was found between enzymic activity and labile sulfide content, at least within the limits of sensitivity of the assays employed. Rhodanese (thiosulfate: cyanide sulfurtransferase (EC 2.8.1.1) purified from bovine liver mitochondria was shown to restore, in the presence of thiosulfate, the activity of the partly inactivated NADH dehydrogenase. Concomitantly, sulfur was transferred from thiosulfate to the flavoprotein and incorporated as acid-labile sulfide. Rhodanese-mediated sulfide transfer was directly demonstrated when the reactivation of NADH dehydrogenase was performed in the presence of radioactive thiosulfate (labeled in the outer sulfur) and the 35S-loaded flavoprotein was re-isolated by gel filtration chromatography. The results indicated that the [35S]sulfide was inserted in NADH dehydrogenase and appeared to constitute the structural basis for the increase in enzymic activity.

Animals↗

PubMed1995

Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice.

Rhodanese (thiosulfate:cyanide sulfurtransferase, E.C. 2.8.1.1), an enzyme involved in heme regulation, showed distinctive mitochondrial and cytoplasmic activities in several models of tumorigenesis. To investigate the basis for these differences, the enzyme was partly purified and characterized from the mitochondrial and cytosolic liver fraction of mice treated with the carcinogen p-dimethyl-aminoazobenzene (DAB). A linear relationship between incubation time and specific activity was observed up to about 30 min for cytosolic enzyme and 15 min for mitochondrial enzyme irrespective of whether or not the enzyme was derived from treated or untreated animals. The optimum incubation temperature was 3 degrees C for the enzyme of both fractions in control animals and 30 degrees C for treated animals in both cases. In control and DAB treated animals the cytoplasmic rhodanese exhibited a maximum at a lower pH than for the mitochondrial enzyme. The enzyme showed typical Michaelis-Menten behavior with cyanide inhibition at concentrations higher than 25 mM for controls and 10 mM for treated animals for both fractions and thiosulfate inhibition at concentrations higher than 100 mM in all cases studied. Km values of 190 and 65.66 mM were obtained for thiosulfate and 6.37 and 9.79 mM for cyanide for both mitochondrial and cytosolic fractions of control animals; while Km values of 31.75 and 4.58 mM were obtained for thiosulfate and 0.61 and 1.11 mM for cyanide in both fractions of treated animals. We demonstrated differences in the kinetics for rhodanese derived from mitochondrial and cytoplasmic fractions of livers taken from tumor bearing mice. These differences might provide an explanation for the abnormalities of heme synthesis previously reported during hepatocarcinogenesis.

Animals↗

PubMed2004

Fatal hydrogen sulfide poisoning at a dye works.

An adult Japanese man (A) entered a pit to remove sludge in a drainage pipe at a dye works in Japan. When he took off a joint of the pipe, the sludge in the pipe flowed into the pit. As he suddenly lost consciousness, three colleagues (B, C, D) entered the pit to rescue him. All of these (A, B, C and D) lost consciousness in the pit, and died soon after the accident. Since hydrogen sulfide gas was detected in the sludge of the pit, gas poisoning was suspected. Toxicological analyses of sulfide and thiosulfate, a metabolite of sulfide, in blood and urine of the victims were made, using the extractive alkylation technique combined with gas chromatography/mass spectrometry. Sulfide and thiosulfate were detected in whole blood of the four workers at levels of 0.32-9.36 mg/l and 0.11-0.23 mmol/l, respectively. These concentrations were at least 6-187 times higher in sulfide and 37-77 times higher in thiosulfate than those in healthy persons, and were similar to values found in fatal cases of hydrogen sulfide poisoning. Thiosulfate was not detected in the urine of four workers, which indicated acute death. Based on these results, all four patients were victims of hydrogen sulfide poisoning, who died soon after the exposure.

Adult↗

PubMed1997

Oxidative metabolism of inorganic sulfur compounds by bacteria.

The history of the elucidation of the microbiology and biochemistry of the oxidation of inorganic sulfur compounds in chemolithotrophic bacteria is briefly reviewed, and the contribution of Martinus Beijerinck to the study of sulfur-oxidizing bacteria highlighted. Recent developments in the biochemistry, enzymology and molecular biology of sulfur oxidation in obligately and facultatively lithotrophic bacteria are summarized, and the existence of at least two major pathways of thiosulfate (sulfur and sulfide) oxidation confirmed. These are identified as the 'Paracoccus sulfur oxidation' (or PSO) pathway and the 'S4intermediate' (or S4I) pathway respectively. The former occurs in organisms such as Paracoccus (Thiobacillus) versutus and P. denitrificans, and possibly in Thiobacillus novellus and Xanthobacter spp. The latter pathway is characteristic of the obligate chemolithotrophs (e.g. Thiobacillus tepidarius, T. neapolitanus, T. ferrooxidans, T. thiooxidans) and facultative species such as T. acidophilus and T. aquaesulis, all of which can produce or oxidize tetrathionate when grown on thiosulfate. The central problem, as yet incompletely resolved in all cases, is the enzymology of the conversion of sulfane-sulfur (as in the outer [S-] atom of thiosulfate [-S-SO3-]), or sulfur itself, to sulfate, and whether sulfite is involved as a free intermediate in this process in all, or only some, cases. The study of inorganic sulfur compound oxidation for energetic purposes in bacteria (i.e. chemolithotrophy and sulfur photolithotrophy) poses challenges for comparative biochemistry. It also provides evidence of convergent evolution among diverse bacterial groups to achieve the end of energy-yielding sulfur compound oxidation (to drive autotrophic growth on carbon dioxide) but using a variety of enzymological systems, which share some common features. Some new data are presented on the oxidation of 35S-thiosulfate, and on the effect of other anions (selenate, molybdate, tungstate, chromate, vanadate) on sulfur compound oxidation, including observations which relate to the roles of polythionates and elemental sulfur as intermediates.

Gram-Negative Aerobic Bacteria↗

PubMed1995

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding.

Efficient renaturation of urea-denatured rhodanese using the chaperonin GroE system requires GroEL, GroES, and ATP. At high concentrations this renaturation also requires the substrate thiosulfate to have been present during GroEL-rhodanese complex formation. When thiosulfate is present the GroEL-rhodanese complex can be concentrated to greater than 1 mg/ml rhodanese with little effect on the efficiency of renaturation. However, if complex is formed in the absence of thiosulfate, renaturation of rhodanese in the presence of thiosulfate shows a critical concentration of approximately 0.4 mg/ml, above which renaturation yields drop dramatically. This critical concentration appears to be related to an aggregation event in the refolding of rhodanese. The nucleotide free or ADP-bound form of GroEL also binds to rhodanese that has been either already renatured or never denatured. The bound rhodanese has no activity but can be released from GroEL with ATP recovering 90% of control activity. The data presented herein support a release and rebinding mechanism for the GroE-assisted refolding of rhodanese. It also suggests GroEL binds several protein folding intermediates along the entire refolding pathway.

Adenosine Diphosphate↗

PubMed1985

Effects of protein-free diet and food deprivation on hepatic rhodanese activity, serum proteins and acute cyanide lethality in mice.

This study was undertaken to evaluate changes in hepatic and extra-hepatic cyanide detoxication resulting from nutritional deficits and any parallel changes in cyanide sensitivity. Male CD-1 mice were fed control diet, control diet in reduced quantities or protein-free diet. After 14 d body weight and relative liver size were lower in the protein-free diet and the food-deprived groups than in the control group. Hepatic and serum protein and albumin concentrations were lower in the protein-free diet group and hepatic protein and albumin concentrations were higher in the food-deprived group than in the control group. Hepatic rhodanese activity was higher in the protein-free diet group than in either of the other two groups. Compared to controls lethality was higher in the protein-free diet group when cyanide was administered in doses of 4 mg/kg body weight alone and 10.7 and 16.0 mg/kg body weight after thiosulfate pretreatment; but only higher in the food-deprived group at the higher dose cyanide given together with thiosulfate. These data suggest that hepatic rhodanese is not principally involved in the detoxication of cyanide even when exogenous thiosulfate is provided, nor does thiosulfate appear to exert its antidotal action by increasing the available cyanide-labile albumin-bound sulfane-sulfur.

Animals↗

PubMed1990

Catabolism of cyst(e)ine by rat renal cortical tubules.

Both cysteinesulfinate-independent and cysteinesulfinate-dependent pathways are involved in the catabolism of cyst(e)ine by freshly isolated rat renal cortical tubules. Sulfate and thiosulfate were shown to be the major sulfur-containing products that accumulated in incubations of renal tubules with 1 mmol/L or 25 mmol/L [35S]cyst(e)ine. Thiosulfate is an intermediate in the oxidation of the sulfide produced by the cysteinesulfinate-independent catabolism of cyst(e)ine by desulfhydration pathway(s), whereas sulfate is formed both by further oxidation of thiosulfate and by oxidation of the sulfite formed by the cysteinesulfinate-transamination pathway. Incubation of renal tubules with propargylglycine inhibited gamma-cystathionase activity by 85%, and this resulted in a 46% decrease in sulfate production and a 68% decrease in thiosulfate production when the treated renal tubules were incubated with 1 mmol/L [35S]cyst(e)ine. Addition of 25 mmol/L unlabeled cysteinesulfinate to create a diluting/trapping pool for [35S]cysteinesulfinate formed from [35S]cysteine resulted in a 53% decrease in [35S]sulfate production in incubations with 1 mmol/L cysteine. Thus, some cyst(e)ine catabolism probably occurred by a cysteinesulfinate-dependent pathway. No production of taurine or hypotaurine was detected in incubations with cyst(e)ine. Thus, cysteinesulfinate formed from cysteine was further catabolized primarily to sulfate instead of to taurine and hypotaurine. Most cyst(e)ine catabolism by the epithelial cells of the renal tubule probably can be accounted for by two pathways: 1) the beta-cleavage of cystine catalyzed by lambda-cystathionase and 2) the formation and transamination of cysteinesulfinate catalyzed by cysteine dioxygenase and aspartate aminotransferase.

Alkynes↗

PubMed1980

Cyanide antidotes and methods of their administration in dogs: a comparative study.

To test the efficacies of various antidotes to cyanide (CN) poisoning, the lethal dose of cyanide in dogs was estimated during constant infusion of potassium cyanide at a rate of 0.1 mg/kg/min. Additionally, arterial blood pressure, right ventricular pressure, heart rate, electrocardiogram, blood-gas and pH values, and whole blood and tissue CN concentrations were measured. The lethal dose in animals whose lungs were ventilated with room air was 2.4 +/- .2 mg/kg (mean +/- SE), while the whole-blood CN concentration was 438 +/- 40 micrograms/dl and the gracilis muscle concentration was 2.0 +/- .3 micrograms/100 g. A low dose of vitamin B12a (100 mg/kg), an infusion of thiosulfate (12 mg/kg/h), or ventilation with 100 per cent O2 increased the amount of CN needed to cause death. A bolus injection of nitrite (5 mg/kg), thiosulfate (150 mg/kg), or cysteine (450 mg/kg) increased the the protection from lethality even further. Protection against CN administration for the total 150-min period of observation was provided by a bolus injection plus a constant infusion of nitrite (5 mg/kg bolus plus 5 mg/kg/h). thiosulfate (30 mg/kg bolus plus 60 mg/kg/h), or vitamin B12a (50 mg/kg bolus plus 100 mg/kg/h). However, nitrite infusion produced high levels of methemoglobin 7.2 +/- 1.1 g/dl, while vitamin B12a infusion and cysteine injection, at the stated doses, did not prevent cyanide-induced circulatory failure. Therefore, thiosulfate appears to be the most effective and safest prophylactic agent against cyanide toxicity in dogs.

Amygdalin↗

PubMed2005

Thioclava pacifica gen. nov., sp. nov., a novel facultatively autotrophic, marine, sulfur-oxidizing bacterium from a near-shore sulfidic hydrothermal area.

Strain TL 2(T) was isolated on mineral medium with thiosulfate from a near-shore sulfidic hydrothermal area in Matupi Harbour on the island of New Britain, Papua New Guinea. The cells varied from long filaments with swollen ends, often aggregated, to short rods, depending on the growth conditions. The bacterium was obligately aerobic and grew autotrophically with thiosulfate as energy source or heterotrophically with organic acids and sugars. In thiosulfate-limited continuous culture, mu(max) and Y(max) for autotrophic growth were 0.1 h(-1) and 3 g protein mol(-1), respectively. From the various reduced sulfur compounds tested, only thiosulfate and sulfide supported active respiration. Inorganic carbon was assimilated via the Calvin cycle. Presence of the 'green'-type of form I RubisCO gene was detected. Growth was possible from 15 to 47 degrees C with an optimum at 35 degrees C, pH 6.5-8.5 with an optimum at pH 8.0, and between 10 and 90 g NaCl l(-1) with an optimum at 35 g l(-1). Phylogenetic analysis based on 16S rRNA and cbbL gene sequences demonstrated that strain TL 2(T) forms a separate lineage within the alpha-3 subdivision of the Proteobacteria, distantly related to the genera Rhodovulum and Rhodobacter. On the basis of these results, a novel genus and species, Thioclava pacifica gen. nov., sp. nov., is proposed to accommodate strain TL 2(T) (= DSM 10166(T) = UNIQEM 229(T)).

Aerobiosis↗

PubMed1977

Rhodanese-Mediated sulfur transfer to succinate dehydrogenase.

The interaction of the sulfurtransferase rhodanese (EC 2.8.1.1) with succinate dehydrogenase (EC 1.3.99.1), yeast alcohol dehydrogenase (EC 1.1.1.1) and bovine serum albumin was studied. Succinate dehydrogenase incorporates the sulfane sulfur of [35S]rhodanese and, in the presence of unlabelled rhodanese, also incorporates that of [35S]thiosulfate. Rhodanese releases most of its transferable sulfur and is re-loaded in the presence of thiosulfate. Rhodanese undergoes similar modifications with yeast alcohol dehydrogenase but this latter does not bind 35S in amounts comparable to those incorporated in succinate dehydrogenase: nearly all the 35S released by [35S]rhodanese is with low-molecular-weight compounds. Bovine serum albumin also binds very little sulfur and [35S]rhodanese present in the reaction mixture does not discharge its radioactive sulfur nor does it take up sulfur from thiosulfate. Sulfur release from rhodanese appears to depend on the presence of - SH groups in the acceptor protein. Sulfur incorporated into succinate dehydrogenase was analytically determined as sulfide. A comparison of the optical spectra of succinate dehydrogenase preparations incubated with or without rhodanese indicates that there is an effect of the sulfurtransferase on the iron-sulfur absorption of the flavorprotein. The interaction of rhodanese with succinate dehydrogenase greatly decreases the catalytic activity of rhodanese with respect to thiocyanate formation. This is attributed to modifications in rhodanese associated with the reduction of sulfane sulfur to sulfide. Thiosulfate in part protects from this deactivation. The reconstitutive capacity of succinate dehydrogenase increased in parallel with sulfur incorporated in that enzyme following its interaction with rhodanese.

Alcohol Oxidoreductases↗

PubMed1988

Physiological characterization of strain DCB-1, a unique dehalogenating sulfidogenic bacterium.

Strain DCB-1 is an obligately anaerobic bacterium which carries out the reductive dehalogenation of halobenzoates and was previously known to grow only on pyruvate plus 20% ruminal fluid. When various electron acceptors were supplied, thiosulfate and sulfite were found to stimulate growth. Sulfide was produced from thiosulfate. Cytochrome c and desulfoviridin were detected. The mol% G+C was 49 (at the thermal denaturation temperature). Of 55 carbon sources tested, only pyruvate supported growth as the sole carbon source in mineral medium. Lactate, acetate, L- and D-malate, glycerol, and L- and D-arabinose stimulated growth when supplemented with 10% ruminal fluid and 20 mM thiosulfate. In mineral medium, pyruvate was converted to acetate and lactate, with small amounts of succinate and fumarate accumulating transiently. During growth with thiosulfate, all of these products accumulated transiently. Addition of excess hydrogen to pyruvate-grown cultures resulted in diversion of carbon to formate, lactate, and butyrate, which caused a decrease in cell yield. We conclude that strain DCB-1 is a new type of sulfidogenic bacterium.

Base Composition↗

PubMed2004

Ferrihydrite-dependent growth of Sulfurospirillum deleyianum through electron transfer via sulfur cycling.

Observations in enrichment cultures of ferric iron-reducing bacteria indicated that ferrihydrite was reduced to ferrous iron minerals via sulfur cycling with sulfide as the reductant. Ferric iron reduction via sulfur cycling was investigated in more detail with Sulfurospirillum deleyianum, which can utilize sulfur or thiosulfate as an electron acceptor. In the presence of cysteine (0.5 or 2 mM) as the sole sulfur source, no (microbial) reduction of ferrihydrite or ferric citrate was observed, indicating that S. deleyianum is unable to use ferric iron as an immediate electron acceptor. However, with thiosulfate at a low concentration (0.05 mM), growth with ferrihydrite (6 mM) was possible and sulfur was cycled up to 60 times. Also, spatially distant ferrihydrite in agar cultures was reduced via diffusible sulfur species. Due to the low concentrations of thiosulfate, S. deleyianum produced only small amounts of sulfide. Obviously, sulfide delivered electrons to ferrihydrite with no or only little precipitation of black iron sulfides. Ferrous iron and oxidized sulfur species were produced instead, and the latter served again as the electron acceptor. These oxidized sulfur species have not yet been identified. However, sulfate and sulfite cannot be major products of ferrihydrite-dependent sulfide oxidation, since neither compound can serve as an electron acceptor for S. deleyianum. Instead, sulfur (elemental S or polysulfides) and/or thiosulfate as oxidized products could complete a sulfur cycle-mediated reduction of ferrihydrite.

Electron Transport↗

PubMed1973

Dissimilatory reduction of inorganic sulfur by facultatively anaerobic marine bacteria.

THREE STRAINS, SELECTED FROM A LARGE NUMBER OF NEWLY ISOLATED, FACULTATIVELY ANAEROBIC MARINE BACTERIA, REDUCED INORGANIC SULFUR COMPOUNDS OTHER THAN SULFATE ANAEROBICALLY IN DEFINED CULTURE MEDIA IN THE FOLLOWING DIFFERENT PATTERNS: (i) sulfite and thiosulfate were reduced to sulfide, and tetrathionate was reduced to thiosulfate; (ii) tetrathionate was reduced to thiosulfate only; or (iii) thiosulfate was reduced to sulfide only when pyruvate was the substrate. Comparison of anaerobic growth in the presence or absence of inorganic sulfur compounds indicated true dissimilatory reductions.

Anaerobiosis↗

PubMed1974

Observations on the bisulfite reductase (P582) isolated from Desulfotomaculum nigrificans.

The bisulfite reductase (P582) from Desulfotomaculum nigrificans was purified to homogeneity as judged by polyacrylamide gel electrophoresis. By colorimetric methods of analysis, the products of bisulfite reduction by this enzyme were determined to be trithionate, thiosulfate, and sulfide. Of these, trithionate was consistently found to be the major product, whereas the latter two were formed in lesser quantities. When [(35)S]bisulfite was incorporated as substrate, no labeled sulfide was detected. Furthermore, when trithionate and thiosulfate were isolated from reaction mixtures and chemically degraded, (35)S was found in all three sulfur atoms of trithionate; however, only the inner sulfur atom of thiosulfate was radioactive. From these data we conclude that the bisulfite reductase of D. nigrificans reduces bisulfite to trithionate and that thiosulfate and sulfide are endogenous side products of the reaction.

Bacteria↗

PubMed1978

Nutritional studies with Pseudomonas aeruginosa grown on inorganic sulfur sources.

Pseudomonas aeruginosa was grown on a succinate-basal salts medium supplemented with various inorganic sulfur compounds as its sole source of sulfur. The organism was able to grow on the sodium salts of sulfide, thiosulfate, tetrathionate, dithionite, metabisulfite, sulfite, or sulfate, but not on those of dithionate. Analyses of the culture media after 24 h of growth indicated accumulation of sulfate from each inorganic sulfur source except sulfate. Manometric studies with resting cells obtained by growth on each of these sulfur sources yielded net oxygen uptake for all substrates except sulfite and dithionate. Similar results were obtained with extracts from these cells by spectrophotometric techniques. Thiosulfate oxidase activity appeared to be induced by growth on sulfide, thiosulfate, or tetrathionate, with little or no activity observed when cells were grown on inorganic sulfur sources of higher oxidative states. Metabisulfite oxidase appeared to be associated with growth on all inorganic sulfur compounds. Rhodanese activity appeared to be constitutively present, and its activity, observed only in soluble fraction, seemed independent of the growth medium employed. Thiosulfate and tetrathionate oxidase activities were studied in greater detail than some of the other sulfur oxidases, and both were found to be distributed between particulate and soluble fractions.

Dithionite↗