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EC Tree
IUBMB Comments The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.
The enzyme appears in viruses and cellular organisms
Synonyms
F420-phenazine oxidoreductase, F420H2 dehydrogenase, F420H2-dehydrogenase,
ffd , Fpo,
FpoAHJKLMN ,
fpoBCDIF ,
FPOF ,
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F420-phenazine oxidoreductase
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F420H2 dehydrogenase
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F420H2-dehydrogenase
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ffd
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Fpo
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FpoAHJKLMN
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fpoBCDIF
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reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420:methanophenazine oxidoreductase
The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.
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oxidized coenzyme F420 + reduced 2,3-dimethyl-1,4-naphthoquinone
reduced coenzyme F420 + oxidized 2,3-dimethyl-1,4-naphthoquinone
oxidized coenzyme F420 + reduced 2-bromophenazine
reduced coenzyme F420 + oxidized 2-bromophenazine
oxidized coenzyme F420 + reduced 2-hydroxyphenazine
reduced coenzyme F420 + oxidized 2-hydroxyphenazine
oxidized coenzyme F420 + reduced ferredoxin
reduced coenzyme F420 + oxidized ferredoxin
oxidized coenzyme F420 + reduced methyl viologen
reduced coenzyme F420 + oxidized methyl viologen
oxidized coenzyme F420 + reduced phenazine
reduced coenzyme F420 + oxidized phenazine
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?
oxidized coenzyme F420 + reduced tetramethyl-4-benzoquinone
reduced coenzyme F420 + oxidized tetramethyl-4-benzoquinone
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reduced coenzyme F420 + 2-bromophenazine
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reduced coenzyme F420 + 2-hydroxyphenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
reduced coenzyme F420 + methyl viologen
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reduced coenzyme F420 + oxidized 2-hydroxyphenazine
oxidized coenzyme F420 + reduced 2-hydroxyphenazine
reduced coenzyme F420 + oxidized metronidazole
oxidized coenzyme F420 + reduced metronidazole
reduced coenzyme F420 + phenazine
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reduced coenzyme F420 + phenazine-1-carboxylic acid
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oxidized coenzyme F420 + reduced 2,3-dimethyl-1,4-naphthoquinone
reduced coenzyme F420 + oxidized 2,3-dimethyl-1,4-naphthoquinone
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oxidized coenzyme F420 + reduced 2,3-dimethyl-1,4-naphthoquinone
reduced coenzyme F420 + oxidized 2,3-dimethyl-1,4-naphthoquinone
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oxidized coenzyme F420 + reduced 2-bromophenazine
reduced coenzyme F420 + oxidized 2-bromophenazine
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oxidized coenzyme F420 + reduced 2-bromophenazine
reduced coenzyme F420 + oxidized 2-bromophenazine
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oxidized coenzyme F420 + reduced 2-hydroxyphenazine
reduced coenzyme F420 + oxidized 2-hydroxyphenazine
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oxidized coenzyme F420 + reduced 2-hydroxyphenazine
reduced coenzyme F420 + oxidized 2-hydroxyphenazine
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oxidized coenzyme F420 + reduced ferredoxin
reduced coenzyme F420 + oxidized ferredoxin
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oxidized coenzyme F420 + reduced ferredoxin
reduced coenzyme F420 + oxidized ferredoxin
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oxidized coenzyme F420 + reduced methyl viologen
reduced coenzyme F420 + oxidized methyl viologen
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oxidized coenzyme F420 + reduced methyl viologen
reduced coenzyme F420 + oxidized methyl viologen
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + oxidized 2-hydroxyphenazine
oxidized coenzyme F420 + reduced 2-hydroxyphenazine
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reduced coenzyme F420 + oxidized 2-hydroxyphenazine
oxidized coenzyme F420 + reduced 2-hydroxyphenazine
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reduced coenzyme F420 + oxidized metronidazole
oxidized coenzyme F420 + reduced metronidazole
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reduced coenzyme F420 + oxidized metronidazole
oxidized coenzyme F420 + reduced metronidazole
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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reduced coenzyme F420 + methanophenazine
oxidized coenzyme F420 + dihydromethanophenazine
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iron-sulfur center
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the enzyme contains iron-sulfur clusters
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Iron
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16 mol non-heme iron per mol enzyme
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0.035
2-hydroxyphenazine
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at pH 7.0 and 25°C
0.25
phenazine
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at pH 7.0 and 25°C
0.0054
reduced coenzyme F420
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at pH 6.8 and 37°C
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25.5
reduced coenzyme F420
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at pH 6.8 and 37°C
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0.6
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with reduced tetramethyl-4-benzoquinone as cosubstrate, at pH 7.0 and 37°C
1.7
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with reduced 2-bromophenazine as cosubstrate, at pH 7.0 and 37°C
1.8
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with phenazine as cosubstrate, at pH 7.0 and 25°C
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with methyl viologen as cosubstrate, at pH 7.0 and 25°C
10.4
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with reduced 2-hydroxyphenazine as cosubstrate, at pH 7.0 and 37°C
4.6
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with phenazine-1-carboxylic acid as cosubstrate, at pH 7.0 and 25°C
8.4
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with 2-bromophenazine as cosubstrate, at pH 7.0 and 25°C
8.8
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with 2-hydroxyphenazine as cosubstrate, at pH 7.0 and 25°C
1.1
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with reduced 2,3-dimethyl-1,4-naphthoquinone as cosubstrate, at pH 7.0 and 37°C
1.1
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with reduced methyl viologen as cosubstrate, at pH 7.0 and 37°C
1.1
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with reduced phenazine as cosubstrate, at pH 7.0 and 37°C
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
40 kDa subunit
UniProt
brenda
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brenda
40 kDa subunit
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
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knockout mutants of the membrane-bound F420 dehydrogenase exhibit severe growth deficiencies with trimethylamine, but not with acetate, as substrates
malfunction
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knockout mutants of the membrane-bound F420 dehydrogenase exhibit severe growth deficiencies with trimethylamine, but not with acetate, as substrates
metabolism
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the enzyme plays a major role in the oxidative part of methylotrophic methanogenesis
metabolism
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the enzyme plays a major role in the oxidative part of methylotrophic methanogenesis
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A0A482V2L2_9EURY
120
0
13539
TrEMBL
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A0A482V4R4_9EURY
594
15
65095
TrEMBL
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A0A482UY07_9EURY
486
12
52546
TrEMBL
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A0A482UY76_9EURY
492
13
53817
TrEMBL
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Q9UXN9_METTI
342
0
37641
TrEMBL
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x * 40000, SDS-PAGE
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x * 45000 + x * 40000 + x * 22000 + x * 18000 + x * 17000, SDS-PAGE
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x * 45000 + x * 40000 + x * 22000 + x * 18000 + x * 17000, SDS-PAGE
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the purified enzyme becomes rapidly inactivated by repeated freezing and thawing
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DEAE-Sephacel column chromatography and EAH-Sepharose column chromatography
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Haase, P.; Deppenmeier, U.; Blaut, M.; Gottschalk, G.
Purification and characterization of F420H2-dehydrogenase from Methanolobus tindarius
Eur. J. Biochem.
203
527-531
1992
Methanolobus tindarius, Methanolobus tindarius DSM 2278
brenda
Welte, C.; Deppenmeier, U.
Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei
FEBS J.
278
1277-1287
2011
Methanosarcina mazei, Methanosarcina mazei DSM 7222
brenda
Baeumer, S.; Murakami, E.; Brodersen, J.; Gottschalk, G.; Ragsdale, S.; Deppenmeier, U.
The F420H2 heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase
FEBS Lett.
428
295-298
1998
Methanosarcina mazei, Methanosarcina mazei Goe1
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brenda
Westenberg, D.; Braune, A.; Ruppert, C.; Müller, V.; Herzberg, C.; Gottschalk, G.; Blaut, M.
The F420H2-dehydrogenase from Methanolobus tindarius cloning of the ffd operon and expression of the genes in Escherichia coli
FEMS Microbiol. Lett.
170
389-398
1999
Methanolobus tindarius (Q9UXN9), Methanolobus tindarius, Methanolobus tindarius DSM 2278 (Q9UXN9)
brenda
Wang, F.P.; Zhang, Y.; Chen, Y.; He, Y.; Qi, J.; Hinrichs, K.U.; Zhang, X.X.; Xiao, X.; Boon, N.
Methanotrophic archaea possessing diverging methane-oxidizing and electron-transporting pathways
ISME J.
8
1069-1078
2014
Methanosarcina sp.
brenda
Abken, H.; Tietze, M.; Brodersen, J.; Baumer, S.; Beifuss, U.; Deppenmeier, U.
Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1
J. Bacteriol.
180
2027-2032
1998
Methanosarcina mazei
brenda
Welte, C.; Deppenmeier, U.
Membrane-bound electron transport in Methanosaeta thermophile
J. Bacteriol.
192
2868-2870
2011
Methanothrix thermoacetophila
brenda
Baumer, S.; Ide, T.; Jacobi, C.; Johann, A.; Gottschalk, G.; Deppenmeier, U.
The F420H2 dehydrogenase from Methanosarcina mazei is a redox-driven proton pump closely related to NADH dehydrogenases
J. Biol. Chem.
275
17968-17973
2000
Methanosarcina mazei, Methanosarcina mazei Goe1
brenda
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1.5.98.3 coenzyme F420:methanophenazine dehydrogenase
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