1.8.2.2: thiosulfate dehydrogenase
This is an abbreviated version!
For detailed information about thiosulfate dehydrogenase, go to the full flat file.
Word Map on EC 1.8.2.2
-
1.8.2.2
-
sulfur
-
sulfite
-
thiobacillus
-
rhodanese
-
sulfur-oxidizing
-
chemolithoautotrophic
-
ferrooxidans
-
vinosum
-
allochromatium
-
paracoccus
-
acidithiobacillus
-
thiooxidans
-
tn5-mob
- 1.8.2.2
- sulfur
- sulfite
- thiobacillus
- rhodanese
-
sulfur-oxidizing
-
chemolithoautotrophic
- ferrooxidans
- vinosum
-
allochromatium
-
paracoccus
-
acidithiobacillus
- thiooxidans
-
tn5-mob
Reaction
2 thiosulfate
+
Synonyms
AFE_0042, Alvin_0091, AvTsdA, C8J_0815, D0Y83_01395, di-heme TsdA, DIE28_04650, diheme cytochrome c TsdA, enzymes, thiosulfate-oxidizing, MpTsdBA, oxidase, thiosulfate, Tat pathway signal sequence domain protein, tetrathionate reductase, tetrathionate synthase, thiosulfate dehydrogenase, thiosulfate oxidase, thiosulfate-acceptor oxidoreductase, thiosulfate-oxidizing enzyme, TSD, TsdA
ECTree
1.8.2.2 thiosulfate dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.8.2.2 - thiosulfate dehydrogenase
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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
tetrathionate + reduced methylviologen
2 thiosulfate + methylviologen
-
-
-
r
thiosulfate + high-potential non-heme iron protein
tetrathionate + reduced high-potential non-heme iron protein
-
-
-
-
r
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
no catalytic activity below 4 mM thiosulfate. Enzyme catalyzes the formation of 1 mol of tetrathionate from 2 mol of thiosulfate
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
r
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
highest activity
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
stoichiometric ratio of conversion is of 1 mole tetrathionate to 2 mol initial thiosulfate. Enzyme can couple thiosulfate oxidation to electron transport to oxygen
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
stoichiometric ratio of conversion is of 1 mole tetrathionate to 2 mol initial thiosulfate. Enzyme can couple thiosulfate oxidation to electron transport to oxygen
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation. A ligand switch from Lys208 to Met209 is observed upon reduction of the enzyme
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
Qipengyuania flava 21-3
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + methyl viologen
very low activity
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + methyl viologen
-
highest activity
-
-
?
thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
-
-
?
thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
activity assay
-
-
ir
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
-
-
-
-
?
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
-
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
phenazine methosulfate and phenazine ethosulfate assayed in the presence of dichlorophenolindophenol and Thialhalivibrio versutus cytochrome c550 support low, but significant enzyme activities
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
Wurster's blue can also serve as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a good electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme is active only with ferricyanide, not with native or mammalian cytochrome c
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme is active only with ferricyanide, not with native or mammalian cytochrome c
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme rapidly reduces high-potential nonheme iron protein in the presence of thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
horse cytochrome c is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c of yeast and cytochrome c of tuna act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a good electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
A-50: once induced to oxidize thiosulfate, also reduces tetrathionate to thiosulfate in the presence of an electron donor such as lactate, the possibility cannot be excluded, that a separate tetrathionate-reducing enzyme is induced
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
ferricyanide or native cytochrome c act as electron acceptors
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
cytochrome c acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
mammalian cytochrome c acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
ferricyanide acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
only native cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome 557 becames reduced when mixed with thiosulfate, enzyme and a trace of cytochrome 553.5, the omission of either the enzyme or cytochrome 553.5 prevents this reduction
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c553.5 acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome 557 becames reduced when mixed with thiosulfate, enzyme and a trace of cytochrome 553.5, the omission of either the enzyme or cytochrome 553.5 prevents this reduction
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c553.5 acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c of yeast is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
horse cytochrome c is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a much better electron acceptor than cytochrome c
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
-
-
-
-
?
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
-
-
-
-
?
additional information
?
-
-
no activity with: pyrrolo-quinoline quinone, methyl- or benzyl viologen, methylthiazol tetrazolium bromide
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
no substrates: sulfite, ubiquinone and horse heart cytochrome c
-
-
?
additional information
?
-
-
no substrates: sulfite, ubiquinone and horse heart cytochrome c
-
-
?
additional information
?
-
the enzyme can reduce neither ubiquinone nor horse heart cytochrome c
-
-
-
additional information
?
-
the enzyme can reduce neither ubiquinone nor horse heart cytochrome c
-
-
-
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with: cytochrome c-552, cytochrome c', cytochrome c-553
-
-
?
additional information
?
-
tetrathionate-dependent methylviologen oxidation and thiosulfate-dependent ferricyanide reduction are measured
-
-
?
additional information
?
-
-
tetrathionate-dependent methylviologen oxidation and thiosulfate-dependent ferricyanide reduction are measured
-
-
?
additional information
?
-
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
-
when coupled with hydrogenase and methyl viologen, the enzyme stoichiometrically reduces thiosulfate to sulfite and sulfide with consumption of hydrogen. No substrates: sulfite or trithionate
-
-
?
additional information
?
-
-
when coupled with hydrogenase and methyl viologen, the enzyme stoichiometrically reduces thiosulfate to sulfite and sulfide with consumption of hydrogen. No substrates: sulfite or trithionate
-
-
?
additional information
?
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
-
no activity with: benzyl viologen, 2,6-dichloroindophenol, 2,6-dichloroindophenol with phenazine methosulfate, 2,6-dichloroindophenol with phenazine ethosulfate, horse heart cytochrome c with phenazine methosulfate, horse heart cytochrome c with phenazine ethosulfate
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with: benzyl viologen, 2,6-dichloroindophenol, 2,6-dichloroindophenol with phenazine methosulfate, 2,6-dichloroindophenol with phenazine ethosulfate, horse heart cytochrome c with phenazine methosulfate, horse heart cytochrome c with phenazine ethosulfate
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
