1.2.7.5: aldehyde ferredoxin oxidoreductase
This is an abbreviated version!
For detailed information about aldehyde ferredoxin oxidoreductase, go to the full flat file.
Word Map on EC 1.2.7.5
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1.2.7.5
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furiosus
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pyrococcus
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hyperthermophilic
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pterins
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acetogenic
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tungstoenzymes
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wood-ljungdahl
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energy-conserving
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molybdopterin
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tungsten-dependent
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ljungdahlii
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crotonaldehyde
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molybdoenzymes
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litoralis
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analysis
- 1.2.7.5
- furiosus
- pyrococcus
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hyperthermophilic
- pterins
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acetogenic
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tungstoenzymes
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wood-ljungdahl
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energy-conserving
- molybdopterin
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tungsten-dependent
- ljungdahlii
- crotonaldehyde
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molybdoenzymes
- litoralis
- analysis
Reaction
Synonyms
aldehyde Fd oxidoreductase, aldehyde ferredoxin oxidoreductase, aldehyde oxidase (ferredoxin), aldehyde oxidoreductase, aldehyde: ferredoxin oxidoreductase, aldehyde:ferredoxin oxidoreductase, AOR, Aor1, Aor2, Aor3, Aor4, aorA, AORAa, Athe_0820, Athe_0821, ebA5355, FOR, formaldehyde ferredoxin oxidoreductase, glyceraldehyde 3-phosphate oxidoreductase, Gor, More, oxidase, aldehyde (ferredoxin), PF0346, phenylacetaldehyde:ferredoxin oxidoreductase, POR, Teth514_1380, tungsten-containing aldehyde ferredoxin oxidoreductases, tungsten-containing aldehyde:ferredoxin oxidoreductase
ECTree
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Metals Ions
Metals Ions on EC 1.2.7.5 - aldehyde ferredoxin oxidoreductase
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Ca2+
Fe2+
Iron
Mg2+
Mo5+
molybdenum can in be incorporated, Mo(V) signal is observed in electron paramagnetic resonance
Molybdenum
Tungsten
additional information
Ca2+
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0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
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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+
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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+
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the [4Fe-4S]-cluster is coordinated by Cys287 of the formaldehyde ferredoxin oxidoreductase and Asp14 of ferredoxin, structure
Fe2+
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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+
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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
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contains 3.3 mol Fe per mol of monomer, the enzyme contains a single [4Fe-4S]2+/1+ cluster per monomer
Iron
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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
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1.5 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Molybdenum
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part of a tungsten-molybdopterin cofactor
Molybdenum
the enzyme with molybdenum has higher redox potential than that with tungsten
Tungsten
B9MQI2; B9MQI1
large subunit GOR-L contains a single tungstopterin site and one iron-sulfur [4Fe-4S] cluster
Tungsten
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contains 0.7 mol tungsten per mol of monomer, the enzyme contains a single tungstopterin cofactor
Tungsten
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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
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electron and redox properties of the 2 tungsten forms with different potential
Tungsten
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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
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electron and redox properties of the 2 tungsten forms with different potential
Tungsten
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each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits
Tungsten
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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
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
Tungsten
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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
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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
an elemental analysis of purified AORAa by ICP-MS analysis reveals the presence of 1.8 W, 38 Fe, 6.2 P, and 2.3 Mg per alpha2beta2gamma2 holoenzyme, whereas no traces of Mo are detected