Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans

Jong, Govardus A.H. de; Hazeu, W.; Bos, P.; Kuenen, J.G.

doi:10.1099/00221287-143-2-499

Cited by 54 publications

(55 citation statements)

References 31 publications

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“…The ensuing formation of trithionate from tetrathionate could be explained by the hydrolysis of tetrathionate to disulphane-monosulphonic acid and the subsequent oxidation of this compound to trithionate. The tetrathionate hydrolase enzyme has been isolated from the cells of A. ferrooxidans, A. thiooxidans, and A. acidophilum [13,14,17]. However, the reaction products differ significantly from those determined for Thiomonas intermedia in this work.…”

Section: Cyclic Degradation Of Thiosulphate and Tetrathionatecontrasting

confidence: 57%

Tetrathionate Disproportionation by Thiomonas intermedia K12

Wentzien

Sand²

2004

Engineering in Life Sciences

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Thiomonas intermedia K12, a moderately acidophilic bacterium, which oxidises sulphur compounds, ± exhibited the capability to use tetrathionate under oxic and anoxic conditions. Whereas under oxic conditions, the reduced sulphur tetrathionate compound was oxidised, under anoxic conditions, the organism disproportionated the compound. In both cases, trithionate and sulphate were produced but in different amounts. The results of the tetrathionate degradation experiments under oxic conditions pointed towards a cyclic degradation process with a transient formation of trithionate and sulphate as the final products, similar to the mechanism described for acidophilic sulphur compound oxidising bacteria. The results of the tetrathionate degradation experiments under anoxic conditions hinted to a partial reduction of tetrathionate to thiosulphate and a fractional oxidation to trithionate and sulphate. 4 M tetrathionate were converted to 6 M thiosulphate, 1 M trithionate, 1 M sulphate, and 8 M protons. The DG 0 ' of this reaction was found to be ±16.1 kJ per mol tetrathionate degraded. Additionally, Thiomonas intermedia K12 grew under anoxic conditions with tetrathionate as the sole energy source. The cell numbers increased from 10 5 as the start value to 10 7 /mL at the end. Organic compounds, excluding traces of yeast extract, did not enhance growth. Therefore, it is proposed that tetrathionate disproportionation is a novel lithotrophic metabolism, which allowed Thiomonas intermedia K12 to survive changing conditions of oxygen supply in sulphur-compound-rich environments and even to grow during this reaction. The extensive sulphur compound analysis was carried out by ion-pair chromatography.

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Section: Cyclic Degradation Of Thiosulphate and Tetrathionatecontrasting

confidence: 57%

Tetrathionate Disproportionation by Thiomonas intermedia K12

Wentzien

Sand²

2004

Engineering in Life Sciences

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“…39) The tetrathionate thus produced was disproportionated by tetrathionate hydrolase to produce thiosulfate, elemental sulfur and sulfate. 14,26) Since the tetrathionate hydrolase reaction does not couple to energy acquisition, the coupling must be done in thiosulfate oxidation. A cytochrome c specifically induced in cells grown on sulfur 5) and a ba 3 -type cytochrome c oxidase proposed by Brasseur et al 30) are probably involved in the coupling.…”

Section: Discussionmentioning

confidence: 99%

“…Although the transfer of electrons from ferrous iron to oxygen has not been conclusively established, the electron transfer pathway is thought to involve two cytochromes c (Cyc2 and Cyc1), a rusticyanin, and an aa 3 -type cytochrome c oxidase. [4][5][6] On the other hand, although some enzyme activities thought to be involved in the aerobic oxidation of elemental sulfur by A. ferrooxidans were detected, [7][8][9][10][11][12][13][14][15][16] the oxidation pathway of elemental sulfur has not yet been clearly elucidated.…”

mentioning

confidence: 99%

Purification and Characterization of Sulfide:Quinone Oxidoreductase from an Acidophilic Iron-Oxidizing Bacterium,Acidithiobacillus ferrooxidans

Wakai

Tsujita

Kikumoto

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…thiooxidans, and At. caldus), [20][21][22][23] in Acidiphilium acidophilum, 24) and in the thermoacidophilic archaeon Ad. ambivalens.…”

Section: )mentioning

confidence: 99%

The sole cysteine residue (Cys301) of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does not play a role in enzyme activity

Kanao

Nakayama

Kato

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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Cysteine residues are absolutely indispensable for the reactions of almost all enzymes involved in the dissimilatory oxidation pathways of reduced inorganic sulfur compounds. Tetrathionate hydrolase from the acidophilic iron- and sulfur-oxidizing bacterium Acidithiobacillus ferrooxidans (Af-Tth) catalyzes tetrathionate hydrolysis to generate elemental sulfur, thiosulfate, and sulfate. Af-Tth is a key enzyme in the dissimilatory sulfur oxidation pathway in this bacterium. Only one cysteine residue (Cys301) has been identified in the deduced amino acid sequence of the Af-Tth gene. In order to clarify the role of the sole cysteine residue, a site-specific mutant enzyme (C301A) was generated. No difference was observed in the retention volumes of the wild-type and mutant Af-Tth enzymes by gel-filtration column chromatography, and surprisingly the enzyme activities measured in the cysteine-deficient and wild-type enzymes were the same. These results suggest that the sole cysteine residue (Cys301) in Af-Tth is involved in neither the tetrathionate hydrolysis reaction nor the subunit assembly. Af-Tth may thus have a novel cysteine-independent reaction mechanism.

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Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans

Cited by 54 publications

References 31 publications

Tetrathionate Disproportionation by Thiomonas intermedia K12

Tetrathionate Disproportionation by Thiomonas intermedia K12

Purification and Characterization of Sulfide:Quinone Oxidoreductase from an Acidophilic Iron-Oxidizing Bacterium,Acidithiobacillus ferrooxidans

The sole cysteine residue (Cys301) of tetrathionate hydrolase from Acidithiobacillus ferrooxidans does not play a role in enzyme activity

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