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hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
SeO32- + a [DsrC protein]-dithiol + 2 reduced methyl viologen + 2 H+
HSe- + a [DsrC protein]-disulfide + 2 oxidized methyl viologen + 3 H2O
-
-
40% of the activity with sulfite
-
?
sulfite + 6 ferrocytochrome c + 6 H+
sulfide + 6 ferricytochrome c + 3 H2O
overall transfer of 6 electrons during the reaction
-
-
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
additional information
?
-
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
-
-
?
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
-
-
50% of the activity with sulfite
-
?
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
-
-
-
-
?
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
-
-
-
-
?
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
-
-
25% of the activity with sulfite
-
?
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
-
-
-
-
?
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
-
-
-
-
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
-
-
overall reaction
-
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
-
-
overall reaction
-
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
-
-
overall reaction
-
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
-
trithionate is the major product, plus formation of thiosulfate and sulfid
-
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
-
trithionate is the major product, plus formation of thiosulfate and sulfid
-
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
-
trithionate is the major product with reduced methyl viologen as electron donor
-
?
additional information
?
-
-
no substrates: S3O62-, S2O32-. Methyl viologen is as effective as ferredoxin in coupling the sulfite reductase with hydrogenase while benzyl viologen is only 16% as effective as ferredoxin. No activity is observed with NAD, NADP, FAD or FMN. Varying the substrate concentration [SO 2-] from 1 to 2.5 micromol affects the stoichiometry of the enzyme reaction by alteration of the ratio of H2 uptake to S2- formed from 2.5:1 to 3.1:1
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
-
two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states
-
-
?
additional information
?
-
-
two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states
-
-
?
additional information
?
-
multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
-
-
?
additional information
?
-
MccA reduces sulfite, but not arsenate, selenate, selenite, hydroxylamine, hydrazine, fumarate, nitrate, thiosulfate, tetrathionate, polysulfide, or Fe(III). Nitrite is reduced only very slowly to ammonium
-
-
?
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evolution
MccA belongs to the genetically diverse family of multiheme c enzymes and has eight heme groups covalently attached to conserved heme-binding motifs in the peptide sequence. Multiheme cytochrome c enzymes show a high conservation of heme group arrangements, but not of sequence, with recurring heme-packing motifs that result in either a parallel or a perpendicular packing of two of the moieties. They catalyse complexmulti-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
additional information
anoxically purified MccA exhibits a 2 to 5.5fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. Presence of two cysteine residues, C399 and C495, juxtaposed at the distal side of the active-site cavity. The active site is a shallow cavity on the distal side of heme 2, lined by residues K208, Y285, Y301, R366 and K393, which are conserved among MccA orthologues
metabolism
-
DsrC is a key protein in dissimilatory sulfite reduction
metabolism
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
metabolism
-
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
-
metabolism
-
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
-
physiological function
Soil bacterium
-
in salt marsh sediments exposed to acid mine drainage for over 100 years, recovered dsrAB sequences of dissimilatory sulfite redactase genes from three sites indicate the dominance of a single Desulfovibrio species. Other major sequence clades are related most closely to Desulfosarcina, Desulfococcus, Desulfobulbus, and Desulfosporosinus species. The presence of metal sulfides with low delta34S values relative to delta34S values of pore water sulfate show that sediment sulfate-reducing bacteria populations are actively reducing sulfate under ambient conditions (pH of about 2), although possibly within less acidic microenvironments. Findings imply a highly dynamic microbially mediated cycling of sulfate and sulfide, and thus the speciation and mobility of chalcophilic contaminant metal(loid)s in acid mine drainage-impacted marsh sediments
physiological function
polar insertion mutations immediately upstream of dsrA, and in dsrB, in the gene cluster dsrABEFHCMK lead to an inability of the cells to oxidize intracellularly stored sulfur. The capability of the mutants to oxidize sulfide, thiosulfate and sulfite under photolithoautotrophic conditions is unaltered. Photoorganoheterotrophic growth is also unaffected
physiological function
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase system. Deletion of dsrM or dsrT, or the two dsrCABL clusters abolishes sulfur globule oxidation and prevents formation of sulfate from sulfide. The DSR system also seems to be involved in the formation of thiosulfate. The dsr mutants incapable of complete substrate oxidation oxidizes sulfide and thiosulfate about twice as fast as the wild-type, while having only slightly lower growth rates of 7080% of wild-type
physiological function
the Epsilonproteobacterium Wolinella succinogenes does not encode a siroheme sulfite reductase and the nrfA gene is not induced during sulfite respiration. Instead, sulfite is reduced by the octaheme c-type cytochrome MccA, with sulfide as the sole product. The enzyme MccA catalyzes the six-electron reduction of sulfite to sulfide, the pivot point of the biogeochemical cycle of the element sulfur for dissimilatory sulfite utilization. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite
physiological function
-
the QmoABC membrane complex is essential for efficient electron delivery to AprAB, in order to sustain catalysis. Direct electron transfer occurs AprAB and the QmoABC complex, coupling the quinone-pool to sulfate reduction
physiological function
the sulfite reductase MET5 gene confers Cys auxotrophy
physiological function
-
polar insertion mutations immediately upstream of dsrA, and in dsrB, in the gene cluster dsrABEFHCMK lead to an inability of the cells to oxidize intracellularly stored sulfur. The capability of the mutants to oxidize sulfide, thiosulfate and sulfite under photolithoautotrophic conditions is unaltered. Photoorganoheterotrophic growth is also unaffected
-
physiological function
-
the sulfite reductase MET5 gene confers Cys auxotrophy
-
physiological function
-
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase system. Deletion of dsrM or dsrT, or the two dsrCABL clusters abolishes sulfur globule oxidation and prevents formation of sulfate from sulfide. The DSR system also seems to be involved in the formation of thiosulfate. The dsr mutants incapable of complete substrate oxidation oxidizes sulfide and thiosulfate about twice as fast as the wild-type, while having only slightly lower growth rates of 7080% of wild-type
-
physiological function
-
the sulfite reductase MET5 gene confers Cys auxotrophy
-
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Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Synthesis, characterization, and stopped-flow kinetics studies of 1,5-IAEDANS-labeled desulfoviridin
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1994
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
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66
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Soil bacterium
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Archaeoglobus profundus (O93650 and O93651), Archaeoglobus profundus, Archaeoglobus profundus DSM 5631 (O93650 and O93651), Desulfofundulus thermocisternus (Q9ZH18 and Q9ZH17), Desulfofundulus thermocisternus
brenda
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Sulfur globule oxidation in green sulfur bacteria is dependent on the dissimilatory sulfite reductase system
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1229-1239
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Chlorobaculum tepidum (Q8K5E9), Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025 (Q8K5E9)
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Intermolecular interaction study of dissimilatory sulfite reductase (DsrAB) from sulfur oxidizing proteobacteria Allchromatium vinosum
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Allochromatium vinosum
-
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Dissimilatory sulfite reductase revisited. The desulfoviridin molecule does contain 20 iron ions, extensively demetallated sirohaem, and an S = 9/2 iron-sulfur cluster
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Desulfovibrio vulgaris
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Pyrobaculum aerophilum (Q8ZUX1), Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523 (Q8ZUX1)
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Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
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Allochromatium vinosum (O33998 and D3RSN2), Allochromatium vinosum DSM 180 (O33998 and D3RSN2)
-
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A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum
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Pyrobaculum islandicum (O33909 and O33910)
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Electron transfer between the QmoABC membrane complex and adenosine 5-phosphosulfate reductase
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Desulfovibrio desulfuricans
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Desulfosporosinus orientis, Desulfovibrio vulgaris, Chlorobium phaeobacteroides, Thermaerobacter marianensis, Desulfitobacterium dichloroeliminans, Chlorobium phaeobacteroides DSM 266, Desulfovibrio vulgaris DP4, Chlorobium phaeobacteroides BS1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfosporosinus orientis DSM 765, Desulfovibrio vulgaris Hildenborough, Thermaerobacter marianensis AB011495
-
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The octahaem MccA is a haem c-copper sulfite reductase
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706-709
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Wolinella succinogenes (Q7MSJ8)
brenda
Nguyen, P.T.; Toh-E, A.; Nguyen, N.H.; Imanishi-Shimizu, Y.; Watanabe, A.; Kamei, K.; Shimizu, K.
Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans
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67
115-128
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Cryptococcus neoformans var. neoformans (Q5K8J1), Cryptococcus neoformans var. neoformans ATCC MYA-565 (Q5K8J1), Cryptococcus neoformans var. neoformans JEC21 (Q5K8J1)
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