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Enzyme Nomenclature
Information on EC 1.8.2.1 - sulfite dehydrogenase (cytochrome)
Word Map on EC 1.8.2.1
- 1.8.2.1
- novella
-
starkeya
- thiosulfate
-
paracoccus
- pantotrophus
-
molybdoenzyme
- molybdopterin
- sulfoacetaldehyde
-
desulfonation
-
sorb
-
chemolithotrophic
- cysteate
-
voltammograms
- food industry
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.2.1
-
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RECOMMENDED NAME
GeneOntology No.
sulfite dehydrogenase (cytochrome)
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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
-
sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme complex that posseses sulfite oxidase activity and thiosulfate-oxidizing activity
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
enzyme enhances the thiosulfate oxidation activity of the core thiosulfate oxidizing multi-enzyme system TOMES with various cytochromes as electron acceptors, enzyme mediates electron transfer between the components of core TOMES and externally added cytochromes
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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 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
-
-
?
additional information
?
-
-
present in taurine-grown cells and effectively absent in acetate grown cells, can be anticipated in both sulfite-generating pathways
-
-
-
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
enzyme is involved in thiosulfate oxidation
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
-
3-5% of the activity with ferricytochrome
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
-
SDH exhibits a high affinity for both sulfite and the electron acceptor cytochrome c and the reaction follows a ping-pong mechanism
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
horse heart cytochrome or yeast cytochrome
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + 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+
-
-
-
-
?
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+
-
-
-
-
?
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
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
-
specific for sulfite
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
cytochrome c from horse heart
-
-
?
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 c + H2O
sulfate + ferrocytochrome c + H+
P07850
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+
Q9LA16
-
-
-
?
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
additional information
-
independent of cytochrome c, assayed with ferricyanide as an electron acceptor
-
cytochrome c-551
-
MW 23000 Da, necessary for the enzyme as an integral part
-
heme
-
the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, 3.53 mol of heme per mol of enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mo
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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INHIBITORS
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
-
Cl-
-
30% electrochemical activity at 100 mM inhibitor concentration, at 50 mM 50% inhibition
p-hydroxymercuribenzoate
-
0.667 mM, 86% loss of activity, inhibition is completely reversed by GSH
phosphate
-
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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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
-
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
-
wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor
0.00605
sulfite
-
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
0.191
sulfite
-
mutant enzyme G473A, pH 8.5, using ferricyanide as the electron acceptor
0.324
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
0.332
sulfite
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236Fyme
1.66
sulfite
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
3.39
sulfite
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
21.2
sulfite
-
mutant enzyme G473W, pH 7.0, using ferricyanide as the electron acceptor
24
sulfite
-
mutant enzyme G473W, pH 8.5, using ferricyanide as the electron acceptor
26.5
sulfite
-
mutant enzyme G473D, pH 7.0, using ferricyanide as the electron acceptor
41.4
sulfite
-
mutant enzyme G473D, pH 8.5, using ferricyanide as the electron acceptor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 3.7
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
10.6
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
35
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
36.19
sulfite
Starkeya novella
-
mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0
40
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
63.5
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
64
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M; 25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M; 25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
86.2
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
158.8
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
293.4
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
345.3
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
410
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
431
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
519
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.84
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
92
11.6
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
92
54.5
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
92
67.7
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
92
251
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
92
950
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
92
1140
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
92
1400
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
92
1500
sulfite
Homo sapiens
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C; mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
92
1500
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
92
1970
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
92
4100
sulfite
Homo sapiens
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
92
4880
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
92
5600
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
92
8420
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
92
15300
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
92
40300
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
92
42700
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
92
75500
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
92
106000
sulfite
Starkeya novella
Q9LA16
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
92
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
8.5
-
the osmium-wired sulfite oxidase shows the same optimum pH (8.5) as in solution with cytochrome c
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is a component of the membrane-associated thiosulfate-oxidizing complex
-
the recombinant enzyme is secreted into the periplasm of Rhodobacter capsulatus
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8800
38815
-
2 * 43897 + 2 * 38815, the 43897 Da subunit contains the 455 Da molybdenum cofactor, the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, electrospray ionization mass spectrometry
40000
40600
42000
43897
-
2 * 43897 + 2 * 38815, the 43897 Da subunit contains the 455 Da molybdenum cofactor, the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, electrospray ionization mass spectrometry
52000
-
1 * 52000, mutant G473D, calculation from amino acid sequence; 2 * 52000, wild type enzyme, sedimentation equilibrium analysis
53500
-
1 * 53500, mutant G473D, gel filtration and sedimentation equilibrium analysis
66600
-
1 * 66600, double mutant R212A/G473D, sedimentation equilibrium analysis
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
monomer
tetramer
heterodimer
-
heterodimeric complex of the catalytic molybdopterin subunit and a c-type cytochrome subunit
monomer
-
1 * 52000, mutant G473D, calculation from amino acid sequence; 1 * 53500, mutant G473D, gel filtration and sedimentation equilibrium analysis; 1 * 54500, mutant G473W, sedimentation equilibrium analysis; 1 * 66600, double mutant R212A/G473D, sedimentation equilibrium analysis
tetramer
-
2 * 43897 + 2 * 38815, the 43897 Da subunit contains the 455 Da molybdenum cofactor, the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, electrospray ionization mass spectrometry; alpha2beta2, 2 * 47000 + 2 * 50000, SDS-PAGE
tetramer
-
2 * 43897 + 2 * 38815, the 43897 Da subunit contains the 455 Da molybdenum cofactor, the 38815 Da subunit consists of a polypeptide and two covalently bound hemes, electrospray ionization mass spectrometry; alpha2beta2, 2 * 47000 + 2 * 50000, SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the C185S variant is crystallized by the hanging drop vapor diffusion method using 15% (v/v) 2-methyl-2,4-pentanediol, 2% PEG 4000 (w/v), and 100 mM sodium acetate (pH 5.0) and in the presence of sulfite using 2% PEG 4000 (w/v), 10% MPD (v/v), 100 mM sodium acetate (pH 5.0) and 0.5 mM sodium sulfite. The C185A variant is crystallized by the sitting drop vapor diffusion method, using 15% (w/v) PEG 4000, 150 mM (NH4)2SO4, and 100 mM MES (pH 6.0)
-
vapour diffusion method. Crystals belong to the space group P2(1)2(1)2, with unit-cell parameters a = 97.5, b = 92.5, c = 55.9
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
58
-
rapid inactivation of oxidized enzyme, substrate-reduced enzyme remains active for more than 1 h
60
100
55
-
complete loss of activity after 5 min, 25% loss of activity after 5 min in presence of 0.05 M sodium sulfite
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
catalytic asctivity is retained upon immobilization of the enzyme on an edge oriented pyrolytic graphite working electrode
-
proteolytic treatment with trypsin at room temperature for up to 5 h at trypsin to enzyme ratios of 1/20 and 1/1 does not affect the activity of the enzyme
-
thawing and refreezing has no effect
treatment with 1-2 mg trypsin per 1.5 mg of protein or 0.1-0.2 mg of pronase or 1.5 mg of protein at 25°C causes decline of activity
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in presence of 20% glycerol stable for several days, without glycerol most of the activity is lost after 48 h
-
-20°C, MES, phosphate, Tris or CAPS buffer, pH 5.5-10.5, for at least 3 months
-
4°C, 10-20% loss of activity after 6 h at room temperature, 80% loss of activity after 5 days
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenyl-Sepharose column chromatography and Superdex 200 16/60 column gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli TP1000 cells
heterologous expression in Rhodobacter capsulatus with the expression vector pDorEX, potentially useful for heterologous expression of multi-subunit proteins containing complex redox cofactors
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C185A
-
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
C185S
-
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
G473A
-
mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type
G473D
-
monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation
G473W
-
monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation
P105A
-
the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme
P105A/P111A
-
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
P111A
-
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
R212A/G473D
-
mutant is able to oligomerize but has undetectable activity, significant random-coil formation
H57A
R55K
-
heme potential is similar to wild-type, the molybdenum redox potential is not affected. Wild-type and mutant show pH dependence of the electrochemical catalytic halfwave potential
R55M
R55Q
-
heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected
Y236F
H57A
mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate
H57A
-
heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent
R55M
mutant with reduced activity, R-55 is an important position close to the substrate binding site, where it makes hydrogen bonds to the equatorial oxo ligand of the molybdenum, to Gln-33, and a nearby water molecule. It also forms a salt bridge, comprising two hydrogen bonds, with propionate-6 of the heme moiety of the cytochrome subunit
R55M
-
heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent
Y236F
-
reduced turnover rates and substrate affinity as well as an altered reactivity toward molecular oxygen as an electron acceptor, unlike the wild type enzyme the mutant enzyme is reoxidized quickly in the presence of molecular oxygen
Y236F
mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
additional information
food industry
-
an electrochemical sulfite biosensor with SDH can be applied to the determination of sulfite in beer and wine samples
food industry
-
the enzyme is used in biosensors for sulfite determination in wine samples
additional information
-
the N-terminal amino acid sequence of the mature SorA from Delftia acidovorans SPH-1 is found in about 500 proteins
additional information
-
N-terminal amino acid sequence of the mature SorA from Cupriavidus necator H16 is currently unique
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.2.1)
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