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At least 19 recordsLinked to original sources
PubMed1991

Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. III. Import, protease processing, and assembly into the cytochrome bc1 complex of iron-sulfur protein lacking the iron-sulfur cluster.

We have used site-directed mutagenesis of the Saccharomyces cerevisiae Rieske iron-sulfur protein gene (RIP 1) to convert cysteines 159, 164, 178, and 180 to serines, and to convert histidines 161 and 181 to arginines. These 4 cysteines and 2 histidines are conserved in all Rieske proteins sequenced to date, and 4 of these 6 residues are thought to ligate the iron-sulfur cluster to the apoprotein. We have also converted histidine 184 to arginine. This histidine is conserved only in respiring organisms. The site-directed mutations of the six fully conserved putative iron-sulfur cluster ligands result in an inactive iron-sulfur protein, lacking iron-sulfur cluster, and failure of the yeast to grow on nonfermentable carbon sources. In contrast, when histidine 184 is replaced by arginine, the iron-sulfur cluster is assembled properly and the yeast grow on nonfermentable carbon sources. The site-directed mutations of the 6 fully conserved residues do not prevent post-translational import of iron-sulfur protein precursor into mitochondria, nor do the mutations prevent processing of iron-sulfur protein precursor to mature size protein by mitochondrial proteases. Optical spectra of mitochondria from the six mutants indicate that cytochrome b is normal, in contrast to the deranged spectrum of cytochrome b which results when the iron-sulfur protein gene is deleted. In addition, mature size iron-sulfur apoprotein is associated with cytochrome bc1 complex purified from a site-directed mutant in which iron-sulfur cluster is not inserted. These results indicate that mature size iron-sulfur apoprotein, lacking iron-sulfur cluster, is inserted into the cytochrome bc1 complex, where it interacts with and preserves the optical properties of cytochrome b. Insertion of the iron-sulfur cluster is not an obligatory prerequisite to processing of the protein to its final size. Either the processing protease cannot distinguish between iron-sulfur protein with or without the iron-sulfur cluster, or insertion of the iron-sulfur cluster occurs after the protein is processed to its mature size, possibly after it is assembled in the cytochrome bc1 complex.

Amino Acid Sequence↗
PubMed1979

Sulfur and methionine metabolism in sheep. I. First approximations of sulfur pools in and sulfur flows from the reticulo-rumen.

Sulfur pools in the rumen and sulfur flows from the rumen were investigated in two experiments with sheep on a diet containing equal parts of oaten and lucerne chaffs. The diet was fed at two levels, either chopped or pelleted, and with intraruminal DL-methionine supplements. Ruminal fluid volumes and fluid flows to the omasum were measured. None of the treatments influenced ruminal fluid volume. Fluid flow to the omasum, however, was increased by increasing dry matter intake (DMI), and was further enhanced by feeding chaffed hay rather than the same materials ground and pelleted; the DL-methionine supplement had no effect. First approximation of the ruminal sulfur pools and of sulfur flows to the omasum were derived from the concentration of sulfur in true digesta and the ruminal fluid volume or fluid flow. Increasing DMI from 500 to 1000 g/day resulted in larger ruminal pools of total (1096 v. 792 mg), neutral (1016 v. 731 mg) and protein (479 v. 419 mg) sulfur, but the reducible sulfur pools were not affected by the level of DMI. Infusions of DL-methionine increased the ruminal sulfide sulfur pool irrespective of level of DMI. The first approximation of total sulfur flow was increased by 1660 mg/day at the higher level of DMI, due mainly to increases of 710 mg S/day as protein sulfur and 859 mg S/day as non-protein neutral sulfur. Flows of inorganic sulfate and ester sulfate sulfur, although small in comparison with organic sulfur flows, increased with level of DMI. Sulfide sulfur flows were also increased at the higher level of DMI, and were almost doubled by intraruminal infusions of DL-methionine.

Animal Feed↗
PubMed2002

Quantitative speciation of sulfur in bacterial sulfur globules: X-ray absorption spectroscopy reveals at least three different species of sulfur.

X-ray absorption near edge structure (XANES) spectroscopy at the sulfur K-edge was applied to probe the speciation of sulfur of metabolically different sulfur-accumulating bacteria in situ. Fitting the spectra using a least-square fitting routine XANES reveals at least three different forms of sulfur in bacterial sulfur globules. Cyclooctasulfur dominates in the sulfur globules of Beggiatoa alba and the very recently described giant bacterium Thiomargarita namibiensis. A second type of sulfur globules is present in Acidithiobacillus ferrooxidans: here the sulfur occurs as polythionates. In contrast, in purple and green sulfur bacteria the sulfur mainly consists of sulfur chains, irrespective of whether it is accumulated in globules inside or outside the cells. These results indicate that the speciation of sulfur in the sulfur globules reflects the different ecological and physiological properties of different metabolic groups of bacteria.

Absorptiometry, Photon↗
PubMed1995

Reconstitution of an iron-sulfur cluster with bound sulfur: a possible source of acid-labile sulfur in biological systems.

The reconstitution of the iron-sulfur cluster of spinach ferredoxin was examined in vitro using low and high molecular bound sulfur components as sulfur donors. Bound sulfur was rapidly converted to acid-labile sulfur to form an iron-sulfur center in the presence of dihydrolipoate and iron. Reconstitution yields of above 95% were obtained with cystine trisulfide (CT, 0.25 mM) and sulfur-bound albumin (SBA, 1.0 mM) at 37 degrees C, pH 7.3, following 60 min incubation. Spectroscopic features and biological activity of the reconstituted ferredoxin were identical to those of the native holo-protein. The acid-labile sulfur content found in the isolated reconstituted ferredoxin was 2 atoms/mol protein, similar to the theoretical value. A possible role for bound sulfur in mammalian cells is indicated and discussed.

Circular Dichroism↗
PubMed1999

In situ analysis of sulfur in the sulfur globules of phototrophic sulfur bacteria by X-ray absorption near edge spectroscopy.

During the oxidation of sulfide and thiosulfate purple and green sulfur bacteria accumulate globules of 'elemental' sulfur. Although essential for a thorough understanding of sulfur metabolism in these organisms, the exact chemical nature of the stored sulfur is still unclear. We applied sulfur K-edge X-ray absorption near edge spectroscopy (XANES) to probe the forms of sulfur in intact cells. Comparing XANES spectra of Allochromatium vinosum, Thiocapsa roseopersicina, Marichromatium purpuratum, Halorhodospira halophila and Chlorobium vibrioforme grown photolithoautotrophically on sulfide with reference probes (fingerprint method), we found sulfur chains with the structure R-S(n)-R. Evidence for the presence of sulfur rings, polythionates and anionic polysulfides in the sulfur globules of these bacteria was not obtained.

Chlorobi↗
PubMed1980

Sulfur--selenium studies in sheep. II. Effect of a dietary sulfur deficiency on selenium and sulfur metabolism in sheep fed varying levels of selenomethionine.

The effect of a sulfur deficiency on the metabolism of selenium and sulfur was investigated in eight merino wethers. The sheep were fed high-sulfur (2 g S/kg) or low-sulfur (0.5 g S/kg) diets for two periods of 35 days each, and received selenium as selenomethionine at dietary concentrations of 0.02, 0.06, 0.09 and 0.67 mg Se/kg. Sheep fed the low-sulfur diet had reduced feed intake, reduced nitrogen, sulfur and selenium balance, but elevated plasma and wool selenium concentrations. Selenium concentrations in organs and tissues of slaughtered animals paralleled the selenium intake of the animal, with the renal cortex containing the highest concentration and bone the lowest. The effect of the 0.5 g S/kg diet on feed intake is in contrast with the results from the previous experiment (White and Somers 1977) using 0.7 g S/kg. It is this difference in fed intake which was responsible for many of the effects on selenium metabolism observed in this experiment. Once the feed intake effects are accounted for, the implications for sulfur--selenium interactions remain as before, i.e. more selenium is incorporated into wool and plasma protein when dietary sulfur is limiting than when it is not.

Animals↗
PubMed2001

Sulfur-to-nitrogen transnitrosation: transfer of nitric oxide from S-nitroso compounds to diethanolamine and the role of intermediate sulfur-to-sulfur transnitrosation.

S-Nitrosothiols are formed in vivo and are involved in NO signaling. We investigated the sulfur-to-nitrogen transnitrosation activity of S-nitrosocysteine, S-nitrosoglutathione, S-nitrosohomocysteine, S-nitrosocysteinylglycine and S-nitroso-N-acetylcysteine in their reaction with the secondary amine diethanolamine in vitro. The resulting N-nitrosodiethanolamine, a strong carcinogen, was formed in yields of up to 11% from S-nitrosocysteine and S-nitrosocysteinylglycine, whereas the transnitrosation activity of the other S-nitroso compounds was weak. However, the addition of L-cysteine to a solution of S-nitrosohomocysteine and diethanolamine accelerated the decomposition of S-nitrosohomocysteine and resulted in a significant formation of N-nitrosodiethanolamine accompanied by the intermediate generation of S-nitrosocysteine. Thus, reactive nitrosothiols can be formed from less reactive analogs via sulfur-to-sulfur transnitrosation. We suggest that this affects regulation of NO trafficking in vivo. The reaction provides an alternative mechanism for the generation of carcinogenic N-nitroso derivatives.

Chromatography, High Pressure Liquid↗
PubMed2002

Limits to sulfur accumulation in transgenic lupin seeds expressing a foreign sulfur-rich protein.

The low sulfur amino acid content of legume seeds restricts their nutritive value for animals. We have investigated the limitations to the accumulation of sulfur amino acids in the storage proteins of narrow leaf lupin (Lupinus angustifolius) seeds. Variation in sulfur supply to lupin plants affected the sulfur amino acid accumulation in the mature seed. However, when sulfur was in abundant supply, it accumulated to a large extent in oxidized form, rather than reduced form, in the seeds. At all but severely limiting sulfur supply, addition of a transgenic (Tg) sink for organic sulfur resulted in an increase in seed sulfur amino acid content. We hypothesize that demand, or sink strength for organic sulfur, which is itself responsive to environmental sulfur supply, was the first limit to the methionine (Met) and cysteine (Cys) content of wild-type lupin seed protein under most growing conditions. In Tg, soil-grown seeds expressing a foreign Met- and Cys-rich protein, decreased pools of free Met, free Cys, and glutathione indicated that the rate of synthesis of sulfur amino acids in the cotyledon had become limiting. Homeostatic mechanisms similar to those mediating the responses of plants to environmental sulfur stress resulted in an adjustment of endogenous protein composition in Tg seeds, even when grown at adequate sulfur supply. Uptake of sulfur by lupin cotyledons, as indicated by total seed sulfur at maturity, responded positively to increased sulfur supply, but not to increased demand in the Tg seeds.

Acetyltransferases↗
PubMed2001

A study on carbothermal reduction of sulfur dioxide to elemental sulfur using oilsands fluid coke.

Experiments and reaction equilibrium calculations were carried out for the SO2 gas and oilsands fluid coke system. The goal was to develop a coke-based sulfur-producing flue gas desulfurization (SP-FGD) process that removes SO2 from flue gases and converts it into elemental sulfur. The conversion of SO2 to elemental sulfur proceeded efficiently at temperatures higher than 600 degrees C, and the sulfur yield reached a maximum (> 95%) at about 700 degrees C. An increase of temperature beyond 700 degrees C enhanced the reduction of product elemental sulfur, resulting in the formation of reduced sulfur species (COS and CS2), which lowered the sulfur yield at 900 degrees C to 90%. Although equilibrium calculations suggest that a lower temperature favors the conversion of SO2 as well as the yield of elemental sulfur, experiments showed no formation of elemental sulfur at 600 degrees C and below, likely due to hindered kinetics. Faster reduction of SO2 was observed at a higher temperature in the range of 700-1000 degrees C. A complete conversion of SO2 was achieved in about 8 s at 700 degrees C. Prolonging the product gas--coke contact, the yield of elemental sulfur decreased due to the formation of COS and CS2 while the SO2 conversion remained complete. Equilibrium calculations suggest that the ultimate yield of elemental sulfur maximizes at the C/SO2 ratio of 1, which represents the stoichiometry of SO2 + C-->CO2 + S. For the C/SO2 ratio < 1, equilibrium calculations predict elemental sulfur and CO2 being major products, suggesting that SO2 + C-->CO2 + S is the predominant reaction if SO2 is in excess. Experiments revealed that elemental sulfur and CO2 were only major products if the conversion of SO2 was incomplete, which is in agreement with the result of the equilibrium modeling.

Air Pollution↗
PubMed2001

Sulfur assimilation in developing lupin cotyledons could contribute significantly to the accumulation of organic sulfur reserves in the seed.

It is currently assumed that the assimilation of sulfur into reduced forms occurs predominantly in the leaves of plants. However, developing seeds have a strong requirement for sulfur amino acids for storage protein synthesis. We have assessed the capacity of developing seeds of narrow-leaf lupin (Lupinus angustifolius) for sulfur assimilation. Cotyledons of developing lupin seeds were able to transfer the sulfur atom from 35S-labeled sulfate into seed proteins in vitro, demonstrating the ability of the developing cotyledons to perform all the steps of sulfur reduction and sulfur amino acid biosynthesis. Oxidized sulfur constituted approximately 30% of the sulfur in mature seeds of lupins grown in the field and almost all of the sulfur detected in phloem exuded from developing pods. The activities of three enzymes of the sulfur amino acid biosynthetic pathway were found in developing cotyledons in quantities theoretically sufficient to account for all of the sulfur amino acids that accumulate in the protein of mature lupin seeds. We conclude that sulfur assimilation by developing cotyledons is likely to be an important source of sulfur amino acids for the synthesis of storage proteins during lupin seed maturation.

Cotyledon↗
PubMed1999

Microbial desulfurization of a crude oil middle-distillate fraction: analysis of the extent of sulfur removal and the effect of removal on remaining sulfur.

Rhodococcus sp. strain ECRD-1 was evaluated for its ability to desulfurize a 232 to 343 degrees C middle-distillate (diesel range) fraction of Oregon basin (OB) crude oil. OB oil was provided as the sole source of sulfur in batch cultures, and the extent of desulfurization and the chemical fate of the residual sulfur in the oil after treatment were determined. Gas chromatography (GC), flame ionization detection, and GC sulfur chemiluminesce detection analysis were used to qualitatively evaluate the effect of Rhodococcus sp. strain ECRD-1 treatment on the hydrocarbon and sulfur content of the oil, respectively. Total sulfur was determined by combustion of samples and measurement of released sulfur dioxide by infrared absorption. Up to 30% of the total sulfur in the middle distillate cut was removed, and compounds across the entire boiling range of the oil were affected. Sulfur K-edge X-ray absorption-edge spectroscopy was used to examine the chemical state of the sulfur remaining in the treated OB oil. Approximately equal amounts of thiophenic and sulfidic sulfur compounds were removed by ECRD-1 treatment, and over 50% of the sulfur remaining after treatment was in an oxidized form. The presence of partially oxidized sulfur compounds indicates that these compounds were en route to desulfurization. Overall, more than two-thirds of the sulfur had been removed or oxidized by the microbial treatment.

Biodegradation, Environmental↗
PubMed2003

The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp.

To identify the actual substrate of the glutathione-dependent sulfur dioxygenase (EC 1.13.11.18) elemental sulfur oxidation of the meso-acidophilic Acidithiobacillus thiooxidans strains DSM 504 and K6, Acidithiobacillus ferrooxidans strain R1 and Acidiphilium acidophilum DSM 700 was analysed. Extraordinarily high specific sulfur dioxygenase activities up to 460 nmol x min(-1) (mg protein)(-1) were found in crude extracts. All cell-free systems oxidized elemental sulfur only via glutathione persulfide (GSSH), a non-enzymic reaction product from glutathione (GSH) and elemental sulfur. Thus, GSH plays a catalytic role in elemental sulfur activation, but is not consumed during enzymic sulfane sulfur oxidation. Sulfite is the first product of sulfur dioxygenase activity; it further reacted non-enzymically to sulfate, thiosulfate or glutathione S-sulfonate (GSSO(-3)). Free sulfide was not oxidized by the sulfur dioxygenase. Persulfide as sulfur donor could not be replaced by other sulfane-sulfur-containing compounds (thiosulfate, polythionates, bisorganyl-polysulfanes or monoarylthiosulfonates). The oxidation of H(2)S by the dioxygenase required GSSG, i.e. the disulfide of GSH, which reacted non-enzymically with sulfide to give GSSH prior to enzymic oxidation. On the basis of these results and previous findings a biochemical model for elemental sulfur and sulfide oxidation in Acidithiobacillus and Acidiphilium spp. is proposed.

Acetobacteraceae↗
PubMed2001

Biological leaching of heavy metals from anaerobically digested sewage sludge using indigenous sulfur-oxidizing bacteria and sulfur waste in a closed system.

The utilization of indigenous sulfur-oxidizing bacteria and sulfur waste was investigated in order to remove heavy metals from anaerobically digested sewage sludge economically. Indigenous sulfur-oxidizing bacteria existing in anaerobically digested sewage sludge were activated by adding elemental sulfur to the sludge and then the bacteria were isolated. It was found that indigenous sulfur-oxidizing bacteria could utilize sulfur waste generated by desulfurization of digestion gas as a substrate. Then, biological leaching of heavy metals from anaerobically digested sewage sludge was carried out using indigenous sulfur-oxidizing bacteria and sulfur waste. By adding sulfur waste to sewage sludge, sulfuric acid was produced by the bacteria and the sludge pH decreased. Heavy metals in sewage sludge were effectively removed owing to the decrease of pH. The optimum amount of sulfur waste added to decrease the pH sufficiently was 5g/L when the sludge concentration was 2%. It was presented that the biological leaching of heavy metals from sewage sludge can be carried out in a closed system, where all required materials are obtained in a sewage treatment plant.

Environmental Pollution↗
PubMed2001

Analysis of sulfur biochemistry of sulfur bacteria using X-ray absorption spectroscopy.

Many sulfide-oxidizing organisms, including the photosynthetic sulfur bacteria, store sulfur in "sulfur globules" that are readily detected microscopically. The chemical form of sulfur in these globules is currently the focus of a debate, because they have been described as "liquid" by some observers, although no known allotrope of sulfur is liquid at physiological temperatures. In the present work we have used sulfur K-edge X-ray absorption spectroscopy to identify and quantify the chemical forms of sulfur in a variety of bacterial cells, including photosynthetic sulfur bacteria. We have also taken advantage of X-ray fluorescence self-absorption to derive estimates of the size and density of the sulfur globules in photosynthetic bacteria. We find that the form of sulfur that most resembles the globule sulfur is simply solid S(8), rather than more exotic forms previously proposed.

Chlorobi↗
PubMed2002

Kinetic studies on elemental sulfur oxidation by Acidithiobacillus ferrooxidans: sulfur limitation and activity of free and adsorbed bacteria.

The kinetics of sulfur oxidation by Acidithiobacillus ferrooxidans in shaking flasks and a 10-L reactor was studied. The observed linearity of growth and sulfur oxidation was explained by sulfur limitation. Total cell yield was not significantly different for exponential growth as compared to growth during the sulfur-limiting phase. Kinetic studies of sulfur oxidation by growing and nongrowing bacteria indicated that both free and adsorbed bacteria oxidize sulfur. Changes in the number of free bacteria rather than cells adsorbed on sulfur were better predictors of the kinetics of sulfur oxidation, indicating that the free bacteria were performing sulfur oxidation. The active growth phase always followed adsorption of bacteria on sulfur; however, the special metabolic role of adsorbed bacteria was unclear. Their activity in sulfur solubilization was considered.

Adsorption↗
PubMed1999

Sulfuric acid on Europa and the radiolytic sulfur cycle.

A comparison of laboratory spectra with Galileo data indicates that hydrated sulfuric acid is present and is a major component of Europa's surface. In addition, this moon's visually dark surface material, which spatially correlates with the sulfuric acid concentration, is identified as radiolytically altered sulfur polymers. Radiolysis of the surface by magnetospheric plasma bombardment continuously cycles sulfur between three forms: sulfuric acid, sulfur dioxide, and sulfur polymers, with sulfuric acid being about 50 times as abundant as the other forms. Enhanced sulfuric acid concentrations are found in Europa's geologically young terrains, suggesting that low-temperature, liquid sulfuric acid may influence geological processes.

Ice↗