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acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + reduced benzyl viologen + H+
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + reduced methyl viologen + H+
-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
crotonaldehyde + CoA + 2 oxidized ferredoxin
crotonate + CO2 + 2 reduced ferredoxin + 2 H+
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + H+ + reduced ferredoxin
-
best substrate
-
-
ir
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
-
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
-
specific activity is 17% compared to the activity with crotonaldehyde
-
-
?
glutaraldehyde + H2O + oxidized methyl viologen
glutarate + H+ + reduced methyl viologen
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
-
-
-
ir
hexanal + H2O + oxidized methyl viologen
hexanoate + H+ + reduced methyl viologen
-
specific activity is 5.7% compared to the activity with crotonaldehyde
-
-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
-
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
-
-
-
r
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
-
-
-
r
additional information
?
-
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
-
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
-
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
low activity
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
low activity, formaldehyde ferredoxin oxidoreductase
-
-
ir
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
-
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
-
artifical electron acceptor
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
formaldehyde and aldehyde ferredoxin oxidoreductases
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
involved in glycolysis
-
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase, no activity
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase, no activity
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
additional information
?
-
-
enzyme shows an active and an inactive form
-
-
?
additional information
?
-
-
enzyme shows an active and an inactive form
-
-
?
additional information
?
-
-
no oxidizing activity with glyceraldehyde-3-phosphate, glyoxylate, glucose, glucose 6-phosphate, CO, H2, formate, pyruvate, 2-oxoglutarate
-
-
?
additional information
?
-
-
NAD(P) is no electron acceptor
-
-
?
additional information
?
-
-
no H2 evolution from reduced methyl viologen
-
-
?
additional information
?
-
-
no activity with CoA
-
-
?
additional information
?
-
-
the enzyme is most active on aldehydes derived from amino acids
-
-
?
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Fe2+
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Mo5+
molybdenum can in be incorporated, Mo(V) signal is observed in electron paramagnetic resonance
Iron
-
each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits. The active-site redox chemistry is based on the pterin part of the cofactor
Tungsten
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Tungsten
the enzyme from Pyrococcus furiosus uses exclusively tungsten to synthesize the catalytically active forms of aldehyde ferredoxin oxidoreductase and active molybdenum- or vanadium-containing isoenzymes are not expressed when the cells are grown in the presence of these other metals
Ca2+
-
binding site, formaldehyde ferredoxin oxidoreductase
Ca2+
-
0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Ca2+
1 Ca2+ per subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit
Fe2+
contains 1 iron-sulfur cluster [4Fe-4S] per subunit
Fe2+
-
electron and redox properties of the [4Fe-4S]-centers
Fe2+
-
6.6 gatoms per 85000g of protein
Fe2+
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Fe2+
contains 1 additional Fe2+ besides the [4Fe-4S]-cluster
Fe2+
-
3.8 gatoms per subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
-
the [4Fe-4S]-cluster is coordinated by Cys287 of the formaldehyde ferredoxin oxidoreductase and Asp14 of ferredoxin, structure
Mg2+
-
1.5 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Mg2+
contains 1 Mg-atom per subunit
Molybdenum
-
part of a tungsten-molybdopterin cofactor
Molybdenum
the enzyme with molybdenum has higher redox potential than that with tungsten
Tungsten
-
-
Tungsten
-
part of a tungsten-molybdopterin cofactor
Tungsten
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Tungsten
-
1.0 gatoms per 85000g of protein
Tungsten
-
electron and redox properties of the 2 tungsten forms with different potential
Tungsten
1 tungsten per subunit
Tungsten
-
0.9 gatom per subunit, formaldehyde ferredoxin oxidoreductase
Tungsten
-
each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits
Tungsten
-
the enzyme contains a tungsten oxo-thiolate center, with two W=O at 1.74 A, approximately three W-S ligands at 2.41 A, and (possibly) a W-O or W-N ligand at 2.1 A. The tungsten site of this enzyme is structurally quite similar to that of molybdenum in the molybdenum oxo-thiolate enzymes
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60
acetaldehyde
pH 8.4, 85°C, benzyl viologen as electron acceptor
0.04
crotonaldehyde
-
pH 8.4, 80°C, with methyl viologen as electron acceptor
0.8
glutaric dialdehyde
pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
1
glyceraldehyde
-
pH 8.4, 65°C, with methyl viologen as electron acceptor
25
Indoleacetaldehyde
pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
15
phenylpropionaldehyde
pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
60
propionaldehyde
pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
8
Succinic semialdehyde
pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
additional information
additional information
-
25
formaldehyde
-
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80°C, with benzyl viologen as electron acceptor
25
formaldehyde
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80°C, with benzyl viologen as electron acceptor
additional information
additional information
-
formaldehyde ferredoxin oxidoreductase, Km for several substrates at different concentrations with purified and sulfide-activated enzyme, overview
-
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
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Mukund, S.; Adams, M.W.W.
The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway
J. Biol. Chem.
266
14208-14216
1991
Pyrococcus furiosus
brenda
Kletzin, A.; Mukund, S.; Kelley-Crouse, T.L.; Chan, M.K.; Rees, D.C.; Adams, M.W.
Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis
J. Bacteriol.
177
4817-4819
1995
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Chan, M.K.; Mukund, S.; Kletzin, A.; Adams, M.W.; Rees, D.C.
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
Science
267
1463-1469
1995
Pyrococcus furiosus
brenda
Koehler, B.P.; Mukund, S.; Conover, R.C.; Dhawan, I.K.; Roy, R.; Adams, M.W.W.; Johnson, M.K.
Spectroscopic characterization of the tungsten and iron centers in aldehyde ferredoxin oxidoreductases from two hyperthermophilic archaea
J. Am. Chem. Soc.
118
12391-12405
1996
Pyrococcus furiosus, Pyrococcus endeavori
-
brenda
Das, S.K.; Biswas, D.; Maiti, R.; Sarkar, S.
Modeling the tungsten sites of inactive and active forms of hyperthermophilic Pyrococcus furiosus aldehyde ferredoxin oxidoreductase
J. Am. Chem. Soc.
118
1387-1397
1996
Pyrococcus furiosus
-
brenda
Roy, R.; Mukund, S.; Schut, G.J.; Dunn, D.M.; Weiss, R.; Adams, M.W.
Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus: the third of a putative five-member tungstoenzyme family
J. Bacteriol.
181
1171-1180
1999
Pyrococcus furiosus
brenda
Hu, Y.; Faham, S.; Roy, R.; Adams, M.W.; Rees, D.C.
Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications
J. Mol. Biol.
286
899-914
1999
Pyrococcus furiosus
brenda
Roy, R.; Menon, A.L.; Adams, M.W.W.
Aldehyde oxidoreductases from Pyrococcus furiosus
Methods Enzymol.
331
132-144
2001
Pyrococcus endeavori, Pyrococcus furiosus, Pyrococcus furiosus (Q51739), Thermococcus litoralis, Thermococcus sp., Thermococcus sp. ES1
brenda
Bevers, L.E.; Bol, E.; Hagedoorn, P.L.; Hagen, W.R.
WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity
J. Bacteriol.
187
7056-7061
2005
Pyrococcus furiosus
brenda
Zhou, Z.H.; Adams, M.W.
Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions
Biochemistry
36
10892-10900
1997
Pyrococcus furiosus
brenda
Arendsen, A.F.; de Vocht, M.; Bulsink, Y.B.M.; Hagen, W.R.
Redox chemistry of biological tungsten: an EPR study of the aldehyde oxidoreductase from Pyrococcus furiosus
Chemistry
1
292-296
1996
Pyrococcus furiosus
-
brenda
George, G.N.; Prince, R.C.; Mukund, S.; Adams, M.W.W.
Aldehyde ferredoxin oxidoreductase from the hyperthermophilic archaebacterium Pyrococcus furiosus contains a tungsten oxo-thiolate cente
J. Am. Chem. Soc.
114
3521-3523
1992
Pyrococcus furiosus
-
brenda
Mukund, S.; Adams, M.W.
Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
178
163-167
1996
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Liao, R.Z.
Why is the molybdenum-substituted tungsten-dependent formaldehyde ferredoxin oxidoreductase not active? A quantum chemical study
J. Biol. Inorg. Chem.
18
175-181
2013
Pyrococcus furiosus (Q8U1K3)
brenda
Liao, R.Z.; Yu, J.G.; Himo, F.
Tungsten-dependent formaldehyde ferredoxin oxidoreductase: reaction mechanism from quantum chemical calculations
J. Inorg. Biochem.
105
927-936
2011
Pyrococcus furiosus (Q8U1K3)
brenda
Basen, M.; Schut, G.J.; Nguyen, D.M.; Lipscomb, G.L.; Benn, R.A.; Prybol, C.J.; Vaccaro, B.J.; Poole, F.L.; Kelly, R.M.; Adams, M.W.
Single gene insertion drives bioalcohol production by a thermophilic archaeon
Proc. Natl. Acad. Sci. USA
111
17618-17623
2014
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (Q51739)
brenda
Sevcenco, A.; Bevers, L.; Pinkse, M.; Krijger, G.; Wolterbeek, H.; Verhaert, P.; Hagen, W.; Hagedoorn, P.
Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus
J. Bacteriol.
192
4143-4152
2010
Pyrococcus furiosus (Q51739)
brenda