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Information on EC 1.8.2.1 - sulfite dehydrogenase (cytochrome)
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1.8.2.1 sulfite dehydrogenase (cytochrome)IUBMB Comments
Associated with cytochrome c-551. The enzyme from the bacterium Starkeya novella contains a molybdopyranopterin cofactor and a smaller monoheme cytochrome c subunit. cf. EC 1.8.5.6, sulfite dehydrogenase (quinone).
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Word Map
- 1.8.2.1
-
starkeya
- novella
- thiosulfate
-
paracoccus
- pantotrophus
-
molybdoenzyme
- sulfoacetaldehyde
-
desulfonation
-
chemolithotrophic
- food industry
The enzyme appears in viruses and cellular organisms
Synonyms
sulfite dehydrogenase, sorab, sir-fp18, sulfite cytochrome c reductase, sulfite oxidoreductase, sulfate oxidase, sulphite:cytochrome c oxidoreductase, sulfite ferricytochrome-c oxidoreductase, multiheme cytochrome c sulfite reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, sulfite
-
-
-
-
SDH
SorA
SorT
sulfate oxidase
sulfite cytochrome c reductase
-
-
-
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sulfite dehydrogenase
sulfite oxidase
sulfite-cytochrome c oxidoreductase
-
-
-
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sulfite: ferricytochrome-c oxidoreductase
sulphite:cytochrome c oxidoreductase
sulfite oxidase
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-
-
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sulphite:cytochrome c oxidoreductase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
ping-pong mechanism
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sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
mechanism of electrochemically mediated, enzyme SorT-catalyzed sulfite oxidation
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sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
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redox reaction
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-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
sulfite:ferricytochrome-c oxidoreductase
Associated with cytochrome c-551. The enzyme from the bacterium Starkeya novella contains a molybdopyranopterin cofactor and a smaller monoheme cytochrome c subunit. cf. EC 1.8.5.6, sulfite dehydrogenase (quinone).
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CAS REGISTRY NUMBER
COMMENTARY
37256-47-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
SO32- + H2O + 2 oxidized cytochrome c
SO42- + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferrocene methanol + H2O
sulfate + 2 reduced ferrocene methanol + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
in the absence of the core thiosulfate oxidizing multi-enzyme system, enzyme catalyzes sulfide-dependent reduction of Chlorobaculum tepidum cytochrome c-554
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
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-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
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-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
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-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
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-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
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-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
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-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
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enzyme is involved in thiosulfate oxidation
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-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
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3-5% of the activity with ferricytochrome
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
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-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
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SDH exhibits a high affinity for both sulfite and the electron acceptor cytochrome c and the reaction follows a ping-pong mechanism
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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horse heart cytochrome or yeast cytochrome
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
ferricytochrome c is the physiological electron acceptor
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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ferricytochrome c is the physiological electron acceptor
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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enzyme is essential for growth with thiosulfate, essential role in lithotrophic sulfur oxidation
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is involved in oxidation of thiosulfate
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is a component of a thiosulfate-oxidizing system
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
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specific for sulfite
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
cytochrome c from horse heart
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-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
oxidative phosphorylation is coupled to sulfite oxidation with a low P/O ratio
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
horse heart cytochrome or yeast cytochrome
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-
?
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
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-
-
-
?
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
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-
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r
additional information
?
-
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present in taurine-grown cells and effectively absent in acetate grown cells, can be anticipated in both sulfite-generating pathways
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-
?
additional information
?
-
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favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
-
-
-
?
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c550 + H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
ferricytochrome c is the physiological electron acceptor
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
ferricytochrome c is the physiological electron acceptor
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
enzyme is essential for growth with thiosulfate, essential role in lithotrophic sulfur oxidation
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is involved in oxidation of thiosulfate
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
the enzyme is a component of a thiosulfate-oxidizing system
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
oxidative phosphorylation is coupled to sulfite oxidation with a low P/O ratio
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c-551
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MW 23000 Da, necessary for the enzyme as an integral part
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heme
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the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, 3.53 mol of heme per mol of enzyme
additional information
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independent of cytochrome c, assayed with ferricyanide as an electron acceptor
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additional information
-
ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mo
Mo4+
-
molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction
Molybdenum
Iron
-
Mo-based and Fe-based voltametric responses from the enzyme in the absence of substrate
Mo
-
consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule
Mo
-
does not play a rate defining role in the catalytic mechanism of SDH before turnover
Mo
-
Mo-PPT binding catalytic subunit (SorA) comprised of an SUOX fold and a dimerization domain
Molybdenum
-
the 43897 Da subunit contains the 455 Da molybdenum cofactor, 1.3 mol of molybdenum per mol of enzyme
Molybdenum
-
the 40600 Da subunit contains the molybdenum cofactor. Mo-based and Fe-based voltametric responses from the enzyme in the absence of substrate
Molybdenum
-
The molybdenum atom of the oxidized enzyme is bound by two ModO ligands at 1.73 aangstroem and three thiolate ModS ligands at 2.42 aangstroem, whereas the reduced enzyme has one oxo at 1.74 aangstroem, one long oxygen at 2.19 aangstroem (characteristic of ModOH2), and three ModS ligands at 2.40 aangstroem
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HPO42-
-
18% electrochemical activity at 100 mM inhibitor concentration, at 20 mM 50% inhibition
NO3-
-
37% electrochemical activity at 100 mM inhibitor concentration, at 3 mM 50% inhibition
additional information
-
CaCl2, MgSO4, ZnSO4, CuSO4, FeCl3, NiCl2 and Na2MoO4 inhibits the reaction by 70% at 0.267 mM, this effect is apparently due to the non-enzymatic oxidation of sulfite with air
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Cl-
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30% electrochemical activity at 100 mM inhibitor concentration, at 50 mM 50% inhibition
p-hydroxymercuribenzoate
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0.667 mM, 86% loss of activity, inhibition is completely reversed by GSH
phosphate
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50 mM, 90% inhibition, uncompetitive with respect to sulfite
SO42-
-
product inhibition, mixed-type non-competitive with respect to sulfite
SO42-
-
19% electrochemical activity at 100 mM inhibitor concentration, at 15 mM 50% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
-
maximal actiovity at final substrate concentrations of 0.02-0.05 M at pH 7.8
additional information
-
SDH emerges at saturating substrate conditions and occurs at a potential of ca. +320 mV vs normal hydrogen electrode
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Kyasanur Forest Disease
Serological response to formolized Kyasanur forest disease virus vaccine in humans at Sagar and Sorab Talukas of Shimoga district.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.58
ferricyanide
-
reaction with ferricyanide or cytochrome c
0.000004
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
0.000007
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
0.0006
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
0.0011
sulfite
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
0.0026
sulfite
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tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
0.0037
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
0.00456
sulfite
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wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor
0.00605
sulfite
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mutant enzyme G473A, pH 7.0, using ferricyanide as the electron acceptor
0.0071
sulfite
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
0.0149
sulfite
-
wild type enzyme, pH 8.6, using ferricyanide as the electron acceptor
0.022
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
0.026
sulfite
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
0.032
sulfite
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.042
sulfite
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
0.086
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme