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Information on EC 1.2.7.5 - aldehyde ferredoxin oxidoreductase and Organism(s) Pyrococcus furiosus and UniProt Accession Q51739
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1.2.7.5 aldehyde ferredoxin oxidoreductaseIUBMB Comments
This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate [see EC 1.2.7.6, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.
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Word Map
- 1.2.7.5
- furiosus
- pyrococcus
-
hyperthermophilic
- pterins
-
acetogenic
-
tungstoenzymes
-
wood-ljungdahl
-
energy-conserving
- molybdopterin
-
tungsten-dependent
- ljungdahlii
- crotonaldehyde
-
molybdoenzymes
- litoralis
- analysis
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aldehyde ferredoxin oxidoreductase, aldehyde:ferredoxin oxidoreductase, glyceraldehyde 3-phosphate oxidoreductase, tungsten-containing aldehyde:ferredoxin oxidoreductase, tungsten-containing aldehyde ferredoxin oxidoreductases, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde oxidase (ferredoxin)
-
-
-
-
AOR
FOR
oxidase, aldehyde (ferredoxin)
-
-
-
-
additional information
AOR
-
-
-
-
additional information
-
formaldehyde ferredoxin oxidoreductase and aldehyde ferredoxin oxidoreductase are 2 separate enzymes
additional information
-
formaldehyde ferredoxin oxidoreductase and aldehyde ferredoxin oxidoreductase are 2 separate enzymes
additional information
-
formaldehyde ferredoxin oxidoreductase and aldehyde ferredoxin oxidoreductase are 2 separate enzymes
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
active site structure
-
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
intermolecular interaction analysis
-
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
substrate binding, catalytic site and reaction mechanism including cofactor action
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
aldehyde:ferredoxin oxidoreductase
This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate [see EC 1.2.7.6, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.
CAS REGISTRY NUMBER
COMMENTARY
138066-90-7
-
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
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+
-
-
-
?
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 ferredoxin
crotonate + H+ + reduced ferredoxin
-
best substrate
-
-
ir
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + 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 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
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
?
-
-
no H2 evolution from reduced methyl viologen
-
-
?
additional information
?
-
-
the enzyme is most active on aldehydes derived from amino acids
-
-
?
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
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
involved in glycolysis
-
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
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tungsten-molybdopterin
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-molybdopterin
-
structural coordination of the tungsten by 4 sulfur ligands in the cofactor
tungsten-molybdopterin
-
interaction with of DXXGL(D,C)X motif and Gly341, Asp343, Asp338, Gly492, Cys494, and Asp489
tungsten-molybdopterin
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-molybdopterin
-
modeling of the tungsten sites of inactive and active enzyme forms
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Tungsten
Ca2+
Fe2+
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
Mg2+
Molybdenum
Tungsten
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+
-
0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit
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+
-
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
Molybdenum
-
part of a tungsten-molybdopterin cofactor
Molybdenum
the enzyme with molybdenum has higher redox potential than that with 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
-
electron and redox properties of the 2 tungsten forms with different potential
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sulfide
4-5fold increase in activity at room temperature and pH 8.0 at 20 mM, in presence of 20 mM dithionite
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53.6
-
purified enzyme, substrate crotonaldehyde with methyl viologen as electron acceptor
additional information
-
formaldehyde ferredoxin oxidoreductase, substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
-
formaldehyde ferredoxin oxidoreductase, activity increases linearly from pH 5.5 to pH 10.0 at 80°C
7 - 8.4
-
activity increases with increasing pH at increasing temperature, nearly no activity below pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 90
-
formaldehyde ferredoxin oxidoreductase, activity increases 4.5fold from 60°C to 90°C at pH 8.4
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the 3 different cofactor model complexes: 1. [Et4N]2[WVIO(1,2-dicyanoethylenedithiolate)2], 2. [Et4N]2[WIVO(1,2-dicyanoethylenedithiolate)2], and 3. [Et4N]2[WVIO(S2)(1,2-dicyanoethylenedithiolate)2], X-ray structure determination and analysis
-
formaldehyde ferredoxin oxidoreductase, purified enzyme, modified melting-point capillary method, room temperature under argon atmosphere, protein solution: 55-65 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM dithionite, 2 mM DTT, 0.2 M KCl, precipitant solution: 30% v/v glycerol, 20% w/v PEG 4000, 0.1 M sodium citrate, pH 5.6, 0.2 M NaCl, several weeks, X-ray structure determination and analysis
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
-
pure enzyme, 5.2 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, exposure to air, less than 20% remaining activity after 5 min, after 10 additional min 10% residual activity is reached, which stays constant for more than 30 min
80
additional information
80
-
formaldehyde ferredoxin oxidoreductase, t1/2: 8 h, in presence of 2 mM dithionite and 2 mM DTT, pH 8.4
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive against O2, dithionite is added to avoid trace contamination with O2 during purification and enzyme assay
-
11938
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, pure enzyme pellet is thawed anaerobically after storage in liquid N2, no loss of activity for several months
-
4°c or 23°C, pure enzyme, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, loss of 25% activity after 6 h under strict anaerobic conditions
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
formaldehyde ferredoxin oxidoreductase, highly reducing and strict anaerobic conditions are required
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity decreases significantly when the organism is grown on maltose plus S(0)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
-
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
-
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
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
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
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
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
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
-
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
-
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
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)
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)
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
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)
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