Sulfur oxidation of Paracoccus pantotrophus: the sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS

Röther, Dagmar; Ringk, Josefina; Friedrich, Cornelius G.

doi:10.1099/mic.0.2008/018655-0

Cited by 17 publications

(12 citation statements)

References 42 publications

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“…Without SoxS the SoxYZ protein is rapidly inactivated but not degraded in vivo which suggests SoxYZ re-activation rather than de novo synthesis. Moreover, SoxY is the target of SoxS as evident from trapping by mixed disulfides of Cys16Ala S [15]. Therefore, it is proposed that the thiol-disulfide oxidoreductase SoxS reduces the interprotein disulfide of one mol of the inactive SoxY-Y(Z) 2 heterotetramer to yield two moles of Sox-YZ.…”

Section: Cys110mentioning

confidence: 99%

“…Inactivation of SoxYZ of P. pantotrophus by blocking the active site Cys110 Y creates the need for either its re-activation or de novo synthesis to maintain the sulfur-oxidizing reaction cycle. SoxYZ is activated by sulfide in vitro and reduction by dithiothreitol keeps the Sox enzyme system active in vivo [11,15]. Sulfide not only reduces the Cys110 Y -Cys110…”

Section: Cys110mentioning

confidence: 99%

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Identification of two inactive forms of the central sulfur cycle protein SoxYZ of Paracoccus pantotrophus

Quentmeier

Friedrich

2008

FEBS Letters

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The central protein of the sulfur-oxidizing enzyme system of Paracoccus pantotrophus, SoxYZ, reacts with three different Sox proteins. Its active site Cys110Y is on the carboxy-terminus of the SoxY subunit. SoxYZ ''as isolated'' consisted mainly of the catalytically inactive SoxY-Y(Z) 2 heterotetramer linked by a Cys110 Y -Cys110 Y interprotein disulfide. Sulfide activated SoxYZ ''as isolated'' 456-fold, reduced the disulfide, and yielded an active SoxYZ heterodimer. The reductant tris(2-carboxyethyl)phosphine (TCEP) inactivated SoxYZ. This form was not re-activated by sulfide, which identified it as a different inactive form. In analytical gel filtration, the elution of ''TCEP-treated'' SoxYZ was retarded compared to active SoxYZ, indicating a conformational change. The possible enzymes involved in the re-activation of each inactive form of SoxYZ are discussed.

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Section: Cys110mentioning

confidence: 99%

Section: Cys110mentioning

confidence: 99%

Identification of two inactive forms of the central sulfur cycle protein SoxYZ of Paracoccus pantotrophus

Quentmeier

Friedrich

2008

FEBS Letters

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“…The outer sulfur atom is oxidized by sulfur dehydrogenase SoxCD, yielding SoxY-cysteine-S-sulfate. Finally, SoxY-cysteine-S-sulfate is hydrolyzed by the dimanganese SoxB protein to yield sulfate and regenerate SoxY for a new reaction cycle of SoxYZ (13, 36). When SoxB or SoxYZ was omitted from the assay mixture, residual H 2 S-dependent activities decreased to approximately 12 or 9%, respectively, that of the mixture of SoxXA, SoxYZ, SoxB, and SoxCD (34).…”

Section: Discussionmentioning

confidence: 99%

Recombinant Sox Enzymes from <i>Paracoccus pantotrophus</i> Degrade Hydrogen Sulfide, a Major Component of Oral Malodor

et al. 2017

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Hydrogen sulfide (H2S) is emitted from industrial activities, and several chemotrophs possessing Sox enzymes are used for its removal. Oral malodor is a common issue in the dental field and major malodorous components are volatile sulfur compounds (VSCs), including H2S and methyl mercaptan. Paracoccus pantotrophus is an aerobic, neutrophilic facultatively autotrophic bacterium that possesses sulfur-oxidizing (Sox) enzymes in order to use sulfur compounds as an energy source. In the present study, we cloned the Sox enzymes of P. pantotrophus GB17 and evaluated their VSC-degrading activities for the prevention of oral malodor. Six genes, soxX, soxY, soxZ, soxA, soxB, and soxCD, were amplified from P. pantotrophus GB17. Each fragment was cloned into a vector for the expression of 6×His-tagged fusion proteins in Escherichia coli. Recombinant Sox (rSox) proteins were purified from whole-cell extracts of E. coli using nickel affinity chromatography. The enzyme mixture was investigated for the degradation of VSCs using gas chromatography. Each of the rSox enzymes was purified to apparent homogeneity, as confirmed by SDS-PAGE. The rSox enzyme mixture degraded H2S in dose- and time-dependent manners. All rSox enzymes were necessary for degrading H2S. The H2S-degrading activities of rSox enzymes were stable at 25–80°C, and the optimum pH was 7.0. The amount of H2S produced by periodontopathic bacteria or oral bacteria collected from human subjects decreased after an incubation with rSox enzymes. These results suggest that the combination of rSox enzymes from P. pantotrophus GB17 is useful for the prevention of oral malodor.

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“…SoxS is exclusively specific for the substrate SoxY of the SoxYZ complex (Rother et al, 2008). In general, thioredoxins are nonspecific with respect to the target proteins, but exhibit a specific thiol-disulfide oxidoreductase redox reaction.…”

Section: Substrate-binding Sitementioning

confidence: 99%

“…Cys13 of SoxS from P. pantotrophus specifically binds to Cys110 Y , as shown by site-directed mutagenesis of the 13 Cys-Leu-Tyr- 16 Cys motif of SoxS (Rother et al, 2008). The thiol of Cys110 Y is subject to chemical modifications by interprotein or mixed disulfide bonds Quentmeier et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

The structure of the periplasmic thiol–disulfide oxidoreductase SoxS fromParacoccus pantotrophusindicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation

Carius

Röther

Friedrich

et al. 2009

Acta Crystallogr D Biol Cryst

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The periplasmic thiol-disulfide oxidoreductase SoxS is beneficial for the sulfur-oxidizing (Sox) phenotype of the facultative chemotrophic bacterium Paracoccus pantotrophus and is not part of the Sox enzyme system. SoxS combines features of thioredoxins, glutaredoxins and the thiol-disulfide oxidoreductases of the Dsb family in structure, target specificity and reaction. The structure of SoxS was solved in oxidized and reduced forms at 2.1 and 1.9 A resolution, respectively. SoxS revealed high structural homology to typical cytoplasmic bacterial thioredoxins. In contrast, SoxS contained the active-site motif Pro-Gly-Cys-Leu-Tyr-Cys that is not present in other thioredoxins. Interestingly, the sequence of this motif is closely related to the Pro-Gly-Cys-Pro-Tyr-Cys sequence of some glutaredoxins and to the Pro-Xaa-Cys-Xaa-Tyr-Cys sequences of some members of the DsbC and DsbG subfamilies of thiol-disulfide oxidoreductases. Furthermore, the proposed substrate of SoxS, the interprotein disulfide of SoxY, Cys110(Y)-Cys110(Y), is structurally similar to oxidized glutathione. However, SoxS is proposed to specifically reduce the interprotein disulfide between two SoxY subunits, releasing a heterodimeric SoxYZ as an active part of the sulfur-oxidation cycle.

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Sulfur oxidation of Paracoccus pantotrophus: the sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS

Abstract: The periplasmic thiol-disulfide oxidoreductase SoxS is essential for chemotrophic growth of Paracoccus pantotrophus with thiosulfate. To trap its periplasmic partner, the cysteine residues of the CysXaaXaaCys motif of SoxS (11 kDa) were changed to alanine by site-directed mutagenesis.

Cited by 17 publications

References 42 publications

Identification of two inactive forms of the central sulfur cycle protein SoxYZ of Paracoccus pantotrophus

Identification of two inactive forms of the central sulfur cycle protein SoxYZ of Paracoccus pantotrophus

Recombinant Sox Enzymes from <i>Paracoccus pantotrophus</i> Degrade Hydrogen Sulfide, a Major Component of Oral Malodor

The structure of the periplasmic thiol–disulfide oxidoreductase SoxS fromParacoccus pantotrophusindicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation

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