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CO2 + methanofuran + reduced acceptor
formylmethanofuran + H2O + acceptor
-
-
-
-
?
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
Formamide + oxidized acceptor
?
Formate + oxidized acceptor
?
formylmethanofuran + H2O + ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
?
formylmethanofuran + H2O + oxidized carbamoylviologen
CO2 + methanofuran + reduced carbamoylviologen
-
-
-
-
r
formylmethanofuran + H2O + oxidized ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
r
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
formylmethanofuran + H2O + oxidized methyl viologen
CO2 + methanofuran + reduced methyl viologen + H+
-
-
-
-
r
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
formylmethanofuran + oxidized acceptor
?
-
formation of formylmethanofuran, which is an intermediate in methanogenesis from CO2
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
formylmethanofuran + oxidized carbamoylmethylviologen + H2O
methanofuran + reduced carbamoylmethylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
N-Furfurylformamide + oxidized acceptor
?
N-Methylformamide + oxidized acceptor
?
additional information
?
-
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
Formamide + oxidized acceptor
?
-
no activity
-
-
?
Formamide + oxidized acceptor
?
-
molybdenum enzyme, 0.1% of the activity relative to formylmethanofuran
-
-
?
Formamide + oxidized acceptor
?
-
no activity
-
-
?
Formate + oxidized acceptor
?
-
no activity
-
-
?
Formate + oxidized acceptor
?
-
molybdenum enzyme, 1% of the activity relative to formylmethanofuran
-
-
?
Formate + oxidized acceptor
?
-
no activity
-
-
?
Formate + oxidized acceptor
?
-
-
-
-
?
Formate + oxidized acceptor
?
-
molybdenum enzyme, 3% of the activity relative to formylmethanofuran
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
r
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
tungsten enzymes are specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
molybdenum enzyme is specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
tungsten enzymes are specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
r
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
molybdenum enzyme, 11% of the activity relative to formylmethanofuran
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
molybdenum enzyme, 1% of the activity relative to formylmethanofuran
-
-
?
N-Methylformamide + oxidized acceptor
?
-
no activity
-
-
?
N-Methylformamide + oxidized acceptor
?
-
molybdenum enzyme, 0.2% of the activity relative to formylmethanofuran
-
-
?
N-Methylformamide + oxidized acceptor
?
-
no activity
-
-
?
additional information
?
-
-
during growth on medium supplemented with selenium only the isoenzyme with selenocysteine at the active site is transcribed. In selenium-deprived medium two tungsten-containing isoenzymes are transcribed
-
-
?
additional information
?
-
-
no activity with coenzyme F420 as electron acceptor
-
-
?
additional information
?
-
-
enzyme is involved in methanogenesis
-
-
?
additional information
?
-
-
key enzyme in methanogenesis
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no reduction of metronidazole, methylene blue, FAD or coenzyme F420 with formylmethanofuran
-
-
?
additional information
?
-
-
initial step of methanogenesis
-
-
?
additional information
?
-
-
the tungsten-containing isoenzyme is constitutively transcribed, the transcription of the molybdenum operon is induced by molybdate
-
-
?
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14000
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
15000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
17000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
17400
calculated from amino acid sequence
200000
-
and MW 400000, native PAGE
21500
calculated from amino acid sequence
22800
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
23100
-
calculated from amino acid sequence
29000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
31600
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
34000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
37000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
400000
-
and MW 200000, native PAGE
50000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
53000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
65100
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
31000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
31000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
31000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
51000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
51000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
64000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
64000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
65000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
65000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
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Vorholt, J.A.; Vaupel, M.; Thauer, R.K.
A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri
Eur. J. Biochem.
236
309-317
1996
Methanosarcina barkeri
brenda
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Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum
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811-818
1994
Methanothermobacter thermautotrophicus
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Formylmethanofuran dehydrogenase from methanogenic archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins
Eur. J. Biochem.
220
477-484
1994
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanothermobacter wolfeii
brenda
Schmitz, R.A.; Albracht, S.P.J.; Thauer, R.K.
A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
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209
1013-1018
1992
Methanothermobacter wolfeii
brenda
Karrasch, M.; Börner, G.; Enssle, M.; Thauer, R.K.
The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor
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194
367-372
1990
Methanosarcina barkeri
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Karrasch, M.; Börner, G.; Enssle, M.; Thauer, R.K.
Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme
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253
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1989
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
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N-Furfurylformamide as a pseudo-substrate for formylmethanofuran converting enzymes from methanogenic bacteria
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268
257-260
1990
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
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Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei
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309
78-81
1992
Methanothermobacter wolfeii
brenda
Börner, G.; Karrasch, M.; Thauer, R.K.
Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)
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290
31-34
1991
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Hochheimer, A.; Heddrich, R.; Thauer, R.K.
The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
Arch. Microbiol.
170
389-393
1998
Methanothermobacter thermautotrophicus, Methanothermobacter wolfeii
brenda
Bertram, P.A.; Schmitz, R.A.; Linder, D.; Thauer, R.K.
Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase
Arch. Microbiol.
161
220-228
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Schmitz, R.A.; Linder, D.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) and formylmethanofuran dehydrogenase from the hyperthermophile Archaeoglobus fulgidus
Arch. Microbiol.
156
427-434
1991
Archaeoglobus fulgidus
-
brenda
Vorholt, J.A.
A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
Mol. Microbiol.
23
1033-1042
1997
Methanopyrus kandleri
brenda
Karrasch, M.; Börner, G.; Thauer, R.K.
The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide
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274
48-52
1990
Methanosarcina barkeri
brenda
Vorholt, J.A.; Thauer, R.K.
The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from Methanogenic archaea
Eur. J. Biochem.
248
919-924
1997
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
brenda
Hochheimer, A.; Linder, D.; Thauer, R.K.; Hedderich, R.
The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation
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242
156-162
1996
Methanothermobacter thermautotrophicus
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de Poorter, L.M.; Geerts, W.G.; Theuvenet, A.P.; Keltjens, J.T.
Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus
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270
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2003
Methanothermobacter thermautotrophicus
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CO2 reduction to the level of formylmethanofuran in Methanosarcina barkeri is non-energy driven when CO is the electron donor
FEMS Microbiol. Lett.
235
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2004
Methanosarcina barkeri
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Tungsten, the surprisingly positively acting heavy metal element for prokaryotes
Ann. N. Y. Acad. Sci.
1125
215-229
2008
Methanothermobacter wolfeii
brenda
Axelrod, H.L.; Das, D.; Abdubek, P.; Astakhova, T.; Bakolitsa, C.; Carlton, D.; Chen, C.; Chiu, H.J.; Clayton, T.; Deller, M.C.; et al
Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved alpha+beta core domain and an auxiliary C-terminal treble-clef zinc finger
Acta Crystallogr. Sect. F
66
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2010
Thermoplasma acidophilum, Desulfitobacterium hafniense (B8FYU2), Syntrophus aciditrophicus (Q2LQ23), Desulfitobacterium hafniense DCB-2 (B8FYU2), Desulfitobacterium hafniense DCB-2, Syntrophus aciditrophicus SB (Q2LQ23), Syntrophus aciditrophicus SB
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Carbon-dependent control of electron transfer and central carbon pathway genes for methane biosynthesis in the Archaean, Methanosarcina acetivorans strain C2A
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2010
Methanosarcina acetivorans
brenda
Costa, K.C.; Wong, P.M.; Wang, T.; Lie, T.J.; Dodsworth, J.A.; Swanson, I.; Burn, J.A.; Hackett, M.; Leigh, J.A.
Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase
Proc. Natl. Acad. Sci. USA
107
11050-11055
2010
Methanothermobacter marburgensis, Methanothermobacter marburgensis S2
brenda
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
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163
112-118
1995
Archaeoglobus fulgidus, Archaeoglobus profundus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus DSM 5631
-
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Pathways of autotrophic CO2 fixation and of dissimilatory nitrate reduction to N2O in Ferroglobus placidus
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167
19-23
1997
Ferroglobus placidus
brenda
Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
brenda
Matschiavelli, N.; Rother, M.
Role of a putative tungsten-dependent formylmethanofuran dehydrogenase in Methanosarcina acetivorans
Arch. Microbiol.
197
379-388
2015
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brenda
Meuer, J.; Kuettner, H.C.; Zhang, J.K.; Hedderich, R.; Metcalf, W.W.
Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
Proc. Natl. Acad. Sci. USA
99
5632-5637
2002
Methanosarcina barkeri
brenda