Information on EC 1.2.7.5 - aldehyde ferredoxin oxidoreductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.2.7.5
-
RECOMMENDED NAME
GeneOntology No.
aldehyde ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Entner Doudoroff pathway
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Metabolic pathways
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Microbial metabolism in diverse environments
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Pentose phosphate pathway
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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 hide
138066-90-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM12254
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Manually annotated by BRENDA team
strain DSM12254
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Manually annotated by BRENDA team
strain AMB-1. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene
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Manually annotated by BRENDA team
strain AMB-1. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene
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-
Manually annotated by BRENDA team
hyperthermophilic archaeon
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Manually annotated by BRENDA team
synthetic construct
-
-
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Manually annotated by BRENDA team
formaldehyde ferredoxin oxidoreductase; hyperthermophilic archaeon
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Manually annotated by BRENDA team
hyperthermophilic archaeon
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Manually annotated by BRENDA team
hyperthermophilic archaeon
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme plays a role in peptide fermentation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen
show the reaction diagram
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at 5% of the activity with crotonaldehyde
-
-
?
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
show the reaction diagram
acetate + H+ + reduced methyl viologen
acetaldehyde + H2O + oxidized methyl viologen
show the reaction diagram
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
benzaldehyde + H2O + oxidized benzyl viologen
benzoate + reduced benzyl viologen
show the reaction diagram
-
at 149% of the activity with crotonaldehyde
-
-
?
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
show the reaction diagram
benzaldehyde + H2O + oxidized ferredoxin
benzoic acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
show the reaction diagram
cinnamaldehyde + H2O + oxidized benzyl viologen
cinnamate + reduced benzyl viologen
show the reaction diagram
-
at 139% of the activity with crotonaldehyde
-
-
?
crotonaldehyde + CoA + 2 oxidized ferredoxin
crotonate + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
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
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-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
show the reaction diagram
crotonaldehyde + H2O + oxidized ferredoxin
pyruvate + H+ + reduced ferredoxin
show the reaction diagram
-
best substrate
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-
ir
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
pyruvate + H+ + reduced methyl viologen
show the reaction diagram
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artifical electron acceptor
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-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
show the reaction diagram
-
specific activity is 17% compared to the activity with crotonaldehyde
-
-
?
glutaraldehyde + H2O + oxidized methyl viologen
glutarate + H+ + reduced methyl viologen
show the reaction diagram
-
-
-
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glutaric dialdehyde + H2O + oxidized benzyl viologen
?
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
show the reaction diagram
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
show the reaction diagram
hexanal + H2O + oxidized methyl viologen
hexanoate + H+ + reduced methyl viologen
show the reaction diagram
-
specific activity is 5.7% compared to the activity with crotonaldehyde
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-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
show the reaction diagram
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
show the reaction diagram
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
show the reaction diagram
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
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-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
show the reaction diagram
salicylaldehyde + H2O + oxidized benzyl viologen
salicylic acid + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
show the reaction diagram
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formaldehyde ferredoxin oxidoreductase
-
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ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
show the reaction diagram
-
involved in glycolysis
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ir
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
form A cofactor
form B cofactor
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in absence of iodine
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molybdopterin
-
-
tungsten cofactor
tungsten-molybdopterin
additional information
synthetic construct
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the active tungsten center is hydrolyzed to the inactive dioxotungsten(VI) center ([WVIO2]2+) in the absence of sulfide
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
Tungsten
Zn2+
-
0.2 gatoms per subunit
additional information
-
contains no detectable molybdenum
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
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competitive to methyl viologen
acetaldehyde
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50% inhibition at 5 mM
aldehydes
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substrate inhibition at high concentrations, overview
arsenite
crotonaldehyde
cyanide
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50% inhibition at 8 mM
iodoacetate
isovalerylaldehyde
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50% inhibition at 4 mM
p-chloromercuribenzoate
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-
phenylacetaldehyde
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50% inhibition at 7 mM
propionaldehyde
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50% inhibition at 0.6 mM
Zn2+
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50% inhibition at 0.25 mM
additional information
-
no effect of CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sulfide
Tungsten
additional information
-
no effect of CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016 - 60
acetaldehyde
1.8
acetate
-
pH 8.4, 85C, benzyl viologen as electron acceptor
0.057
benzaldehyde
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pH 8.4, 85C, benzyl viologen as electron acceptor
0.17
benzyl viologen
-
pH 8.4, 85C, with crotonaldehyde
0.04 - 0.3
crotonaldehyde
0.01
Ferredoxin
-
ES-1 ferredoxin; pH 8.4, 85C, with crotonaldehyde
-
1.42 - 25
formaldehyde
0.8
glutaric dialdehyde
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.2 - 1
glyceraldehyde
0.05 - 25
Indoleacetaldehyde
0.028
isovalerylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
2.9
methyl viologen
-
pH 8.4, 85C, with crotonaldehyde
0.076
phenylacetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
15
phenylpropionaldehyde
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.15 - 60
propionaldehyde
0.065
Salicylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
8
Succinic semialdehyde
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
343
acetaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
1.6
acetate
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
720
benzaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
250
benzyl viologen
Thermococcus sp.
-
pH 8.4, 85C, with crotonaldehyde
22 - 269
crotonaldehyde
270
Ferredoxin
Thermococcus sp.
-
ES-1 ferredoxin, pH 8.4, 85C, with crotonaldehyde
-
950
formaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
2.8
glyceraldehyde
Thermococcus sp.
-
pH 8.4, 45C, benzyl viologen as electron acceptor
55
Indoleacetaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
272
isovalerylaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
62
methyl viologen
Thermococcus sp.
-
pH 8.4, 85C, with crotonaldehyde
960
phenylacetaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
1100
propionaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
13
Salicylaldehyde
Thermococcus sp.
-
pH 8.4, 85C, benzyl viologen as electron acceptor
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Pyrococcus furiosus
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pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
65C, pH not specified in the publication
42
-
purified formaldehyde ferredoxin oxidoreductase
53.6
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purified enzyme, substrate crotonaldehyde with methyl viologen as electron acceptor
238
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purified enzyme
additional information
-
formaldehyde ferredoxin oxidoreductase, substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
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formaldehyde ferredoxin oxidoreductase, activity increases linearly from pH 5.5 to pH 10.0 at 80C
6 - 10
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oxidation of acetaldehyde with benzyl viologen as electron acceptor
7 - 8.4
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activity increases with increasing pH at increasing temperature, nearly no activity below pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 90
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formaldehyde ferredoxin oxidoreductase, activity increases 4.5fold from 60C to 90C at pH 8.4
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
-
gel filtration
105000
-
gel filtration
110000
-
gel filtration
130000
-
gel filtration
134000
-
crystal structure
200000
-
gel filtration
275000
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formaldehyde ferredoxin oxidoreductase, gel filtration
280000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
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1 * 80000, SDS-PAGE
tetramer
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4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
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
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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
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X-ray crystal structure determination and analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% glycerol and 2 mM DTT stabilize during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aldehyde ferredoxin oxidoreductase, t1/2: 30 min at 23 C
644691
formaldehyde ferredoxin oxidoreductase, t1/2: 9 h at 23C
644691
sensitive against O2, dithionite is added to avoid trace contamination with O2 during purification and enzyme assay
-
11938
very sensitive to O2, after 1 h at 60C 3% activity remains, after 1 h at 4C 39% activity remains
-
11935
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196C, pure enzyme pellet is thawed anaerobically after storage in liquid N2, no loss of activity for several months
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4c or 23C, 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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 120fold, to homogeneity
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enzyme from vanadium- and molybdenum-grown cells
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formaldehyde and aldehyde ferredoxin oxidoreductase; formaldehyde ferredoxin oxidoreductase, highly reducing and strict anaerobic conditions are required
formaldehyde ferredoxin oxidoreductase, 17fold
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formaldehyde ferredoxin oxidoreductase, highly reducing and strict anaerobic conditions are required
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to homogeneity under strict anaerobic conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthetic construct
-
in situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes that model the proposed active-site structure for the AOR family of tungsten enzymes. The complexes are characterized by UV-vis, electrospray ionization mass spectrometry, IR, and resonance Raman spectroscopies and are found to mimic the coordination environment including the W=E (E=O, S) bond strengths and hydrolytic reactions of the tungsten center of the AOR family
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