BRENDA - Enzyme Database
show all sequences of 1.2.7.5

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

Roy, R.; Mukund, S.; Schut, G.J.; Dunn, D.M.; Weiss, R.; Adams, M.W.; J. Bacteriol. 181, 1171-1180 (1999)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Sulfide
activation of formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
General Stability
General Stability
Organism
10% glycerol and 2 mM DTT stabilize during purification
Pyrococcus furiosus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
formaldehyde ferredoxin oxidoreductase, Km for several substrates at different concentrations with purified and sulfide-activated enzyme, overview
Pyrococcus furiosus
25
-
formaldehyde
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80°C, with benzyl viologen as electron acceptor
Pyrococcus furiosus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Fe2+
3.8 gatoms per subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Mg2+
1.5 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Tungsten
0.9 gatom per subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
Pyrococcus furiosus
275000
-
formaldehyde ferredoxin oxidoreductase, gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an aldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
-
an acid + H+ + reduced ferredoxin
-
Pyrococcus furiosus
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus furiosus
-
contains a formaldehyde and an aldehyde ferredoxin oxidoreductase; genes aor and for; hyperthermophilic archaeon; strain DSM 3638
-
Purification (Commentary)
Commentary
Organism
formaldehyde ferredoxin oxidoreductase, 17fold
Pyrococcus furiosus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
formaldehyde ferredoxin oxidoreductase, substrate specificity
Pyrococcus furiosus
42
-
purified formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
acetate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
acetaldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
acetate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
an aldehyde + H2O + oxidized ferredoxin
-
644689
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
?
an aldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
644689
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
low activity
644689
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
crotonaldehyde + H2O + oxidized benzyl viologen
low activity, formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
pyruvate + H+ + reduced benzyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
formate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
formaldehyde + H2O + oxidized ferredoxin
formaldehyde and aldehyde ferredoxin oxidoreductases
644689
Pyrococcus furiosus
formate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase, no activity
644689
Pyrococcus furiosus
isovalerate + H+ + reduced benzyl viologen
-
-
-
-
propionaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
propionate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
propionaldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
propionate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
Subunits
Subunits
Commentary
Organism
tetramer
4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Pyrococcus furiosus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
90
formaldehyde ferredoxin oxidoreductase, activity increases 4.5fold from 60°C to 90°C at pH 8.4
Pyrococcus furiosus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the enzyme is thermostable
Pyrococcus furiosus
80
-
formaldehyde ferredoxin oxidoreductase, t1/2: 8 h, in presence of 2 mM dithionite and 2 mM DTT, pH 8.4
Pyrococcus furiosus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
assay at
Pyrococcus furiosus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
formaldehyde ferredoxin oxidoreductase, activity increases linearly from pH 5.5 to pH 10.0 at 80°C
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Pyrococcus furiosus
form A cofactor
formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Sulfide
activation of formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Pyrococcus furiosus
form A cofactor
formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
General Stability (protein specific)
General Stability
Organism
10% glycerol and 2 mM DTT stabilize during purification
Pyrococcus furiosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
formaldehyde ferredoxin oxidoreductase, Km for several substrates at different concentrations with purified and sulfide-activated enzyme, overview
Pyrococcus furiosus
25
-
formaldehyde
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80°C, with benzyl viologen as electron acceptor
Pyrococcus furiosus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Fe2+
3.8 gatoms per subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Mg2+
1.5 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Tungsten
0.9 gatom per subunit, formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
Pyrococcus furiosus
275000
-
formaldehyde ferredoxin oxidoreductase, gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an aldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
-
an acid + H+ + reduced ferredoxin
-
Pyrococcus furiosus
?
Purification (Commentary) (protein specific)
Commentary
Organism
formaldehyde ferredoxin oxidoreductase, 17fold
Pyrococcus furiosus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
formaldehyde ferredoxin oxidoreductase, substrate specificity
Pyrococcus furiosus
42
-
purified formaldehyde ferredoxin oxidoreductase
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
acetate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
acetaldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
acetate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
an aldehyde + H2O + oxidized ferredoxin
-
644689
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
?
an aldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
644689
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
low activity
644689
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
crotonaldehyde + H2O + oxidized benzyl viologen
low activity, formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
pyruvate + H+ + reduced benzyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
formate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
formaldehyde + H2O + oxidized ferredoxin
formaldehyde and aldehyde ferredoxin oxidoreductases
644689
Pyrococcus furiosus
formate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase, no activity
644689
Pyrococcus furiosus
isovalerate + H+ + reduced benzyl viologen
-
-
-
-
propionaldehyde + H2O + oxidized benzyl viologen
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
propionate + H+ + reduced benzyl viologen
-
644689
Pyrococcus furiosus
ir
propionaldehyde + H2O + oxidized ferredoxin
formaldehyde ferredoxin oxidoreductase
644689
Pyrococcus furiosus
propionate + H+ + reduced ferredoxin
-
644689
Pyrococcus furiosus
ir
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Pyrococcus furiosus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
90
formaldehyde ferredoxin oxidoreductase, activity increases 4.5fold from 60°C to 90°C at pH 8.4
Pyrococcus furiosus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the enzyme is thermostable
Pyrococcus furiosus
80
-
formaldehyde ferredoxin oxidoreductase, t1/2: 8 h, in presence of 2 mM dithionite and 2 mM DTT, pH 8.4
Pyrococcus furiosus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
assay at
Pyrococcus furiosus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
formaldehyde ferredoxin oxidoreductase, activity increases linearly from pH 5.5 to pH 10.0 at 80°C
Pyrococcus furiosus
Other publictions for EC 1.2.7.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740953
Liew
Metabolic engineering of Clost ...
Clostridium autoethanogenum
Metab. Eng.
40
104-114
2017
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1
1
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740209
Ammam
Effect of tungstate on acetate ...
Sporomusa ovata, Sporomusa ovata DSM-2662
Biotechnol. Biofuels
9
163
2016
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737164
Basen
Single gene insertion drives b ...
Pyrococcus furiosus
Proc. Natl. Acad. Sci. USA
111
17618-17623
2014
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740626
Debnar-Daumler
Simultaneous involvement of a ...
Aromatoleum aromaticum
J. Bacteriol.
196
483-492
2014
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2
1
1
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3
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1
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8
1
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722823
Liao
Why is the molybdenum-substitu ...
Pyrococcus furiosus
J. Biol. Inorg. Chem.
18
175-181
2013
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722893
Liao
Tungsten-dependent formaldehyd ...
Pyrococcus furiosus
J. Inorg. Biochem.
105
927-936
2011
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745210
Sevcenco
Molybdenum incorporation in t ...
Pyrococcus furiosus
J. Bacteriol.
192
4143-4152
2010
-
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1
1
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1
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1
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1
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1
1
1
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692610
Sugimoto
In situ generation of oxo-sulf ...
synthetic construct
Inorg. Chem.
46
8460-8462
2007
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1
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675237
Thapper
Biochemical and spectroscopic ...
Desulfovibrio aminophilus, Desulfovibrio aminophilus DSM 12254
J. Inorg. Biochem.
100
44-50
2006
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2
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5
1
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5
1
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656293
Hagedoorn
Purification and characterizat ...
Pyrobaculum aerophilum
J. Biol. Inorg. Chem.
10
259-269
2005
-
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-
-
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1
-
3
2
-
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4
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1
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1
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6
1
1
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1
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2
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1
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1
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6
1
1
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674251
Bevers
WOR5, a novel tungsten-contain ...
Pyrococcus furiosus
J. Bacteriol.
187
7056-7061
2005
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4
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1
1
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654430
Wahyudi
Characterization of aldehyde f ...
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1
Biochem. Biophys. Res. Commun.
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223-229
2003
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644691
Roy
Aldehyde oxidoreductases from ...
Pyrococcus endeavori, Pyrococcus furiosus, Thermococcus litoralis, Thermococcus sp., Thermococcus sp. ES1
Methods Enzymol.
331
132-144
2001
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745202
Adams
Key role for sulfur in peptid ...
Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
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644689
Roy
Purification and molecular cha ...
Pyrococcus furiosus
J. Bacteriol.
181
1171-1180
1999
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644690
Hu
Formaldehyde ferredoxin oxidor ...
Pyrococcus furiosus
J. Mol. Biol.
286
899-914
1999
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721578
Zhou
Site-directed mutations of the ...
Pyrococcus furiosus
Biochemistry
36
10892-10900
1997
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644687
Koehler
-
Spectroscopic characterization ...
Pyrococcus endeavori, Pyrococcus furiosus
J. Am. Chem. Soc.
118
12391-12405
1996
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644688
Das
-
Modeling the tungsten sites of ...
Pyrococcus furiosus
J. Am. Chem. Soc.
118
1387-1397
1996
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722057
Arendsen
-
Redox chemistry of biological ...
Pyrococcus furiosus
Chemistry
1
292-296
1996
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722490
Mukund
Molybdenum and vanadium do not ...
Pyrococcus furiosus
J. Bacteriol.
178
163-167
1996
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11935
Heider
Purification, characterization ...
Thermococcus sp., Thermococcus sp. ES1
J. Bacteriol.
177
4757-4764
1995
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644684
Kletzin
Molecular characterization of ...
Pyrococcus furiosus
J. Bacteriol.
177
4817-4819
1995
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644686
Chan
Structure of a hyperthermophil ...
Pyrococcus furiosus
Science
267
1463-1469
1995
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722438
George
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Aldehyde ferredoxin oxidoreduc ...
Pyrococcus furiosus
J. Am. Chem. Soc.
114
3521-3523
1992
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11938
Mukund
The novel tungsten-iron-sulfur ...
Pyrococcus furiosus
J. Biol. Chem.
266
14208-14216
1991
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