Thiosulfate, polythionates and elemental sulfur assimilation and reduction in the bacterial world

Faou, A Le

doi:10.1016/0378-1097(90)90688-m

Cited by 47 publications

(10 citation statements)

References 159 publications

(310 reference statements)

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“…Although only a few S°-reducing mesophiles are known (see [92]), the reduction of S ° to H2S is virtually a universal characteristic of the hyperthermophiles. The majority are obligately dependent upon S ° reduction as an energy source ( Table 1).…”

Section: Mechanisms Of S ° Reduction By P Furiosusmentioning

confidence: 99%

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

Adams

1994

FEMS Microbiology Reviews

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Hyperthermophiles are a recently discovered group of microorganisms that grow at and above 90 degrees C. They currently comprise over 20 different genera, and except for two novel bacteria, all are classified as Archaea. The majority of these organisms are obligately anaerobic heterotrophs that reduce elemental sulfur (S degree) to H2S. The best studied from a biochemical perspective are the archaeon, Pyrococcus furiosus, and the bacterium, Thermotoga maritima, both of which are saccharolytic. P. furiosus is thought to contain a new type of Entner-Doudoroff pathway for the conversion of carbohydrates ultimately to acetate, H2 and CO2. The pathway is independent of nicotinamide nucleotides and involves novel types of ferredoxin-linked oxidoreductases, one of which has tungsten, a rarely used element, as a prosthetic group. The only site of energy conservation is at the level of acetyl CoA, which is the presence of ADP and phosphate is converted to acetate and ATP in a single step. In contrast, T. maritima utilizes a conventional Embden-Meyerhof pathway for sugar oxidation. P. furiosus also utilizes peptides as a sole carbon and energy source. Amino acid oxidation is thought to involve glutamate dehydrogenase together with at least three types of novel ferredoxin-linked oxidoreductases which catalyze the oxidation of 2-ketoglutarate, aryl pyruvates and formaldehyde. One of these enzymes also utilizes tungsten. In P. furiosus, virtually all of the reductant that is generated during the catabolism of both carbohydrates and peptides is channeled to a cytoplasmic hydrogenase. This enzyme is now termed sulhydrogenase, as it reduces both protons to H2 and S degrees (or polysulfide) to H2S. S degrees reduction appears to lead to the conservation of energy in P. furiosus but not in T. maritima, although the mechanism by which this occurs is not known.

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Section: Mechanisms Of S ° Reduction By P Furiosusmentioning

confidence: 99%

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

Adams

1994

FEMS Microbiology Reviews

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“…However, the physiological role of these enzymes remained dubious. Enzymes exhibiting thiosulphate sulphur transferase activity occur in many bacteria and eukarya not able to oxidize thiosulphate (Westley et al, 1984;Le Faou et al, 1990) and genetic studies were lacking. During the past several years data accumulated that cast further doubt on an important role of rhodanese or thiosulphate reductase during thiosulphate oxidation in sulphur-storing bacteria: Clusters of sox genes were identified in thiosulphate-oxidizing green sulphur bacteria (Eisen et al, 2002;Verté et al, 2002) and PCR analyses proved the existence of the highly con-served soxB gene also in other thiosulphate-utilizing but not in non-thiosulphate-utilizing strains of green sulphur bacteria (Petri et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Hensen

Sperling

Trüper

et al. 2006

Molecular Microbiology

167

192

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SummaryTwo different pathways for thiosulphate oxidation are present in the purple sulphur bacterium Allochromatium vinosum: oxidation to tetrathionate and complete oxidation to sulphate with obligatory formation of sulphur globules as intermediates. The tetrathionate:sulphate ratio is strongly pH-dependent with tetrathionate formation being preferred under acidic conditions. Thiosulphate dehydrogenase, a constitutively expressed monomeric 30 kDa c-type cytochrome with a pH optimum at pH 4.2 catalyses tetrathionate formation. A periplasmic thiosulphateoxidizing multienzyme complex (Sox) has been described to be responsible for formation of sulphate from thiosulphate in chemotrophic and phototrophic sulphur oxidizers that do not form sulphur deposits. In the sulphur-storing A. vinosum we identified five sox genes in two independent loci (soxBXA and soxYZ). For SoxA a thiosulphate-dependent induction of expression, above a low constitutive level, was observed. Three sox-encoded proteins were purified: the heterodimeric c-type cytochrome SoxXA, the monomeric SoxB and the heterodimeric SoxYZ. Gene inactivation and complementation experiments proved these proteins to be indispensable for thiosulphate oxidation to sulphate. The intermediary formation of sulphur globules in A. vinosum appears to be related to the lack of soxCD genes, the products of which are proposed to oxidize SoxY-bound sulphane sulphur. In their absence the latter is instead transferred to growing sulphur globules.

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“…It has been repeatedly assumed that such compounds are formed in natural environments during the chemical oxidation of free or solid phase sulfides [3][4][5]. A great variety of aerobic and anaerobic bacteria are known which utilize these sulfur oxyanions either as electron donors or acceptors during the oxidative or reductive reactions of their energy metabolism [6][7][8][9]. Many aspects of the microbial metabolism of sulfur oxyanions have been studied in detail.…”

Section: Introductionmentioning

confidence: 99%

Determination of tetrathionate and thiosulfate in natural samples and microbial cultures by a new, fast and sensitive ion chromatographic technique

Bak

1993

FEMS Microbiology Ecology

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A new isocratlc ion chromatographic techmque ~s described for the sensitwe measurement of tetrathlonate, tnthlonate and thlosulfate. The sulfur oxyanions were separated on a polymer-coated, silica-based anion-exchange column and dtrectly detected by UV absorption at 216 nm. Aqueous saline acetonitrile/methanol mixtures were used as eluent. The three amons could be quannfied m less than 10 mln w~th detection hmlts of about 0.6 pmol for tetrath~onate and of 40 and 10 pmol for trithlonate and thlosulfate, respectively. The retention times of tetrathionate responded to changes of the solvent concentratton, whereas the elution of thiosulfate depended predominatly on the ~omc strenght of the eluent. Starting at the lowest detectable concentrations, calibration curves for all three compounds were hnear over a concentration range of three orders of magnitude. The analys~s of freshwater and sahne samples worked equally well. Since contact of the eluent with metallic components caused shifts in retention times during operation, the solvent dehvery system had to consist of plastic material. Examples of application are given for determination of tetrath~onate and thiosulfate m natural samples and for the turnover of these two compounds m sediment slurries and anaerobic enrichment cultures.

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Thiosulfate, polythionates and elemental sulfur assimilation and reduction in the bacterial world

Cited by 47 publications

References 159 publications

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum

Determination of tetrathionate and thiosulfate in natural samples and microbial cultures by a new, fast and sensitive ion chromatographic technique

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