The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c.
The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c.
subunit SoxC first comes in contact with water and thereby breaks down the oxygen-hydrogen bond in water. The oxygen, which is liberated as oxide anion (O2-), then forms covalent bond with the protein bound sulfur atom and liberates two electrons, which are then taken up by the di-heme cytochrome c protein SoxD
the complete sulfur-oxidizing enzyme system reconstituted from subunits Sox(CD)2, SoxYZ, SoxXA, and SoxB accepts hydrogen sulfide, sulfur, thiosulfate, and sulfite for reduction of horse cytochrome c
subunit SoxD harbors two heme domains. 3.65 mol of heme per mol of enzyme tetramer. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system
the side chains of His297, Arg316 and the main chain nitrogen atoms of Ser327 and Lys360 are involved in H-bonding with the oxygen atoms of the heme propionate group
molybdenum cofactor exists as low- and high-pH species with g and A(95,97Mo) matrices nearly identical to those of sulfite oxidase. No sulfite-induced reduction to MoV is detected. The outer coordination sphere controls substrate binding in SoxCD, permitting access only to protein-bound sulfur via the C-terminal tail of SoxY
sulfite oxidase-type molybdenum cofactor in subunit SoxC, residue Arg114 involved in the first oxidation step is in close proximity to the molybdenum atiom
overview on structure and function of the soxXYZABCD gene cluster and comparison with other organisms. The Sox system reconstituted from SoxXA, SoxYZ, SoxB, and SoxCD mediates thiosulfate-, sulfite-, sulfur-, and hydrogen sulfide-dependent cytochrome c reduction. SoxCD acts as a dehydrogenase at a protein-bound sulfur atom
recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture degrades H2S in dose- and time-dependent manners. All recombinant Sox enzymes are necessary for degrading H2S
the sulfur-oxidizing enzyme system reconstituted from proteins SoxXA, SoxYZ, SoxB, and SoxCD releases 8 mol of electrons per mol of thiosulfate. Omission of SoxCD from the system reduces the rate of thiosulfate oxidation by 70% and the electron yield to 2 mol of electrons per mol of thiosulfate. SoxCD is also required for the maximum rates of hydrogen sulfide-, sulfur-, and sulfite-dependent cytochrome c reduction, which are 18, 25, and 60% of the rate with SoxCD included, respectively
the sulfur-oxidizing enzyme system reconstituted from proteins SoxXA, SoxYZ, SoxB, and SoxCD releases 8 mol of electrons per mol of thiosulfate. Omission of SoxCD from the system reduces the rate of thiosulfate oxidation by 70% and the electron yield to 2 mol of electrons per mol of thiosulfate. SoxCD is also required for the maximum rates of hydrogen sulfide-, sulfur-, and sulfite-dependent cytochrome c reduction, which are 18, 25, and 60% of the rate with SoxCD included, respectively
recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture degrades H2S in dose- and time-dependent manners. All recombinant Sox enzymes are necessary for degrading H2S
dimerization of subunit SoxD helps to bring the two distant heme groups in close proximity, which helps in the transport of electrons efficiently from one part of the protein to the other part, structure modeling data. subunits SoxC and SoxD interact strongly with each other
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking studies and comparison of the molecular mechanism of sulfur oxidation process in Dechloromonas aromatica and Thiobacillus denitrificans, the latter using proteins SoxAX instead of proteins SoxCD for recycling of SoxY. The SoxYZ protein of SoxCD lacking Thiobacillus denitrificans is more stable and interactive, in comparison with the SoxYZ complex from SoxCD-possessing Dechloromonas aromatica
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons
homology modeling of structure. SoxD belongs to the di-heme cytochrome c family of electron transport proteins whereas soxC gene product (SoxC) is a sulfur dehydrogenase
construction of a mutant lacking the heme-2 domain. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system, kinetic data are similar to wild-type
the amount of H2S produced by periodontopathic bacteria or oral bacteria collected from human subjects decreases after an incubation with recombinant Sox enzymes. The combination of recombinant Sox enzymes is useful for the prevention of oral malodor
the amount of H2S produced by periodontopathic bacteria or oral bacteria collected from human subjects decreases after an incubation with recombinant Sox enzymes. The combination of recombinant Sox enzymes is useful for the prevention of oral malodor
Structural insight into SoxC and SoxD interaction and their role in electron transport process in the novel global sulfur cycle in Paracoccus pantotrophus
Insight into the conformational variations in SoxYZ protein complex from two different members of the beta-proteobacterial family involved in sulfur oxidation
Interdiscip. Sci.
9
309-321
2017
Dechloromonas aromatica (Q47BB7 and Q47BB8), Dechloromonas aromatica
Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17