Purification and paritial characterization of a thermostable trithionate hydrolase from the acidophilic sulphur oxidizer <i>Thiobacillus acidophilus</i>

Meulenberg, R.; Pronk, Jack T.; Frank, J.; Hazeu, W.; Bos, P.; Kuenen, J.G.

doi:10.1111/j.1432-1033.1992.tb17298.x

Cited by 32 publications

(31 citation statements)

References 37 publications

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“…This is an unusual enzymatic reaction that has only otherwise been suggested for enzymes designated as trithionate or tetrathionate hydrolases (15)(16)(17)(18). The thiosulfohydrolase activity proposed for SoxB has yet to be directly demonstrated.…”

Section: Soxy-shmentioning

confidence: 99%

Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase SoxB

Sauvé

Roversi

Leath

et al. 2009

Journal of Biological Chemistry

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SoxB is an essential component of the bacterial Sox sulfur oxidation pathway. SoxB contains a di-manganese(II) site and is proposed to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. A direct assay for SoxB activity is described. The structure of recombinant Thermus thermophilus SoxB was determined by x-ray crystallography to a resolution of 1.5 Å . Structures were also determined for SoxB in complex with the substrate analogue thiosulfate and in complex with the product sulfate. A mechanistic model for SoxB is proposed based on these structures.

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Section: Soxy-shmentioning

confidence: 99%

Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase SoxB

Sauvé

Roversi

Leath

et al. 2009

Journal of Biological Chemistry

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“…Further studies such as X-ray crystallography of the purified protein may resolve the reason behind the heat tolerance. Similar studies of thermostable enzymes of mesophilic bacteria have been conducted for trithionate hydrolase of Acidithiobacillus acidophilus and sulfur oxygenase reductase of Halothiobacillus neapolitanus (Meulenberg et al, 1992;Veith et al, 2012).…”

mentioning

confidence: 59%

“…This result suggested that the SCNase may have a special property of cold inactivation and heat reactivation. The characteristic of cold inactivation was also found in other enzymes such as E. coli tryptophanase (Erez et al, 1998), trithionate hydrolase of Thiobacillus acidophilus (reclassified as Acidiphilium acidophilum) (Meulenberg et al, 1992) and ribulose-1,5-biphosphate carboxylase-oxygenase from tobacco leaf (Chollet & Anderson, 1977). In the latter, the cold inactivation was the result of partial dissociation of the hydrophobic catalytic subunits of the enzyme (Chollet & Anderson, 1977).…”

mentioning

confidence: 79%

Cloning and expression of a gene encoding a novel thermostable thiocyanate-degrading enzyme from a mesophilic alphaproteobacteria strain THI201

et al. 2013

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Strain THI201, a member of the alphaproteobacteria, is a novel thiocyanate (SCN " )-degrading bacterium isolated from lake water enriched with potassium thiocyanate (KSCN). This bacterium carries the enzyme thiocyanate hydrolase (SCNase) that hydrolyses thiocyanate to carbonyl sulfide and ammonia. Characterization of both native and recombinant SCNase revealed properties different from known SCNases regarding subunit structure and thermostability: SCNase of strain THI201 was composed of a single protein and thermostable. We cloned and sequenced the corresponding gene and determined a protein of 457 amino acids of molecular mass 50 267 Da. Presence of a twin-arginine (Tat) signal sequence of 32 amino acids was found upstream of SCNase. The deduced amino acid sequence of SCNase showed 83 % identity to that of a putative uncharacterized protein of Thiobacillus denitrificans ATCC 25259, but no significant identity to those of three subunits of SCNase from Thiobacillus thioparus strain THI115. The specific activities of native and recombinant enzyme were 0.32 and 4-15 mmol min "1 (mg protein), respectively. The maximum activity of SCNase was found in the temperature range 30-70 6C. The thiocyanate-hydrolysing activity in both enzymes was decreased by freezethawing, although 25-100 % of the activity of recombinant protein could be retrieved by treating the enzyme at 60 6C for 15 min. Furthermore, both native and recombinant enzymes retained the activity after pre-treatment of the protein solution at temperatures up to 70 6C.

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“…The thiosulfateoxidizing enzyme was successfully solubilized from intact cells by passing the acidic ammonium sulfate suspension through a French pressure cell following the procedures for trithionate hydrolase isolation from Thiobacillus acidophilus (Meulenberg et al 1992), although this latter enzyme activity was not found in our sulfur-grown T. thiooxidans. 2.…”

Section: Thiosulfate Oxidation By the Acidic Extractmentioning

confidence: 99%

Thiosulfate oxidation by sulfur-grown Thiobacillus thiooxidans cells, cell-free extracts, and thiosulfate-oxidizing enzyme

Chan¹,

Suzuki²

1994

Can. J. Microbiol.

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CHAN, C.W., and SUZUKI, I. 1994. Thiosulfate oxidation by sulfur-grown Thiobacillus thiooxidans cells, cell-free extracts, and thiosulfate-oxidizing enzyme. Can. J. Microbiol. 40: 81 6-822. The oxidation of thiosulfate by Thiobacillus thioosidans grown on sulfur was studied in cells, cell-free extracts, and a thiosulfate-oxidizing enzyme system. Thiosulfate was oxidized to tetrathionate by cells treated with N-ethylmaleimide with a pH optimum at 2.3. The cell-free extracts also oxidized thiosulfate with the same pH optimum and 0 2 consumption. Untreated cells, OII the other hand, oxidized thiosulfate to sulfite in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide, an inhibitor of sulfite oxidation. The cells treated with N-ethylmaleimide showed two K,,, values for thiosulfate while the cell-free system showed only one K,. The K,,, value for thiosulfate generally increased with the increasing pH. A soluble thiosulfate-oxidizing enzyme system was extracted from the cells at pH 2.5 in the presence of 1 M ammonium sulfate by passage through a French pressure cell. The system contained a native cytochrome c that was reduced by thiosulfate at pH 2.5 and a thiosulfate-ferricyanide oxidoreductase activity with a pH optimum around 2.0. The acidic extract also contained-a component that reduced horse heart cytochrome c at a neutral pH. The reduction at an acidic pH required sulfite. -free extracts, and thiosulfate-oxidizing enzyme. Can. J. Microbiol. 40 : 81 6-822. L'oxydation du thiosulfate par le Thiobacillus thioosidarls cultivC sur du soufre a Ct C CtudiCe dans des cellules, des extraits acellulaires et un systbme enzymatique oxydant le thiosulfate. Le thiosulfate a CtC oxydC en tCtrathionate par des cellules traitCes avec du N-CthylmalCimide B un pH optimum de 2,3. Les extraits acellulaires ont Cgalement oxydC le thiosulfate au meme pH et avec la meme consommation d'oxyg$ne. Par ailleurs, les cellules non-traitCes ont oxydC le thiosulfate en sulfite en du N-oxyde de 2-rz-heptyl-4-hydroxyquinoline, un inhibiteur de I'oxydation du sulfite. Les cellules traitCes au N-CthylmalCimide ont montrC deux valeurs de K,,, pour le thiosulfate tandis que le systkme acellulaire en a montrt qu'une seule. Dans l'ensemble, la valeurde K,,, pour le thiosulfate a augment6 suivant l'augmentation du pH. Un systbme enzymatique soluble oxydant le thiosulfate a CtC extrait, a la suite d'un passage dans une presse de French, a partir des cellules ti pH 2,5 en prksence de 1 M sulfate d'ammonium.Le systbme contenait un cytochrome c nature1 qui a CtC rCduit par le thiosulfate B pH 2,5 et une activitC oxydorCductase de thiosulfate-ferricyanure avec un pH optimum de 2,O environ. L'extrait acide contenait aussi un composant qui a rCduit ti pH neutre le cytochrome c extrait du coeur de cheval. La rkduction pH acide a requis du sulfite.

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Purification and paritial characterization of a thermostable trithionate hydrolase from the acidophilic sulphur oxidizer Thiobacillus acidophilus

Cited by 32 publications

References 37 publications

Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase SoxB

Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase SoxB

Cloning and expression of a gene encoding a novel thermostable thiocyanate-degrading enzyme from a mesophilic alphaproteobacteria strain THI201

Thiosulfate oxidation by sulfur-grown Thiobacillus thiooxidans cells, cell-free extracts, and thiosulfate-oxidizing enzyme

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