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IUBMB Comments The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si -face specific with respect to C-5 of coenzyme F420 .
The expected taxonomic range for this enzyme is: Methanomada group
Synonyms FprA, more
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FprA
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2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O
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reduced coenzyme F420:oxygen oxidoreductase
The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C-5 of coenzyme F420 [2].
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2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme does not use NADH or NADPH as electron donor or H2O2 as electron acceptor Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme does not use NADH or NADPH as electron donor or H2O2 as electron acceptor Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: - Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme does not use NADH or NADPH as electron donor or H2O2 as electron acceptor Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is Si-face specific with respect to C5 of coenzyme F420 Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the F420H2 oxidase reaction represents a ping-pong process where, in a first reaction, four electrons from the diferrous di-iron and FMNH2 are transferred to the dioxygen, thereby forming two water molecules without the release of reactive oxygen species, and in a second reaction, the two redox centers are re-reduced by two hydride transfer reactions between reduced coenzyme F420 and FMN Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme does not use NADH or NADPH as electron donor or H2O2 as electron acceptor Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is Si-face specific with respect to C5 of coenzyme F420 Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: - Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the F420H2 oxidase reaction represents a ping-pong process where, in a first reaction, four electrons from the diferrous di-iron and FMNH2 are transferred to the dioxygen, thereby forming two water molecules without the release of reactive oxygen species, and in a second reaction, the two redox centers are re-reduced by two hydride transfer reactions between reduced coenzyme F420 and FMN Products: -
?
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2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: - Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: the enzyme is involved in O2 detoxification Products: -
?
2 reduced coenzyme F420 + O2
2 oxidized coenzyme F420 + 2 H2O
Substrates: - Products: -
?
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FMN
the 45000 Da protein contains 1 FMN per mol
FMN
the 45000 Da protein contains 1 FMN per mol
FMN
the enzyme contains FMN
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Iron
the 45000 Da protein harbors a binuclear iron center
Fe2+
the 45000 Da protein harbors a binuclear iron center
Fe2+
di-iron center, in the active reduced state [Fe(II)Fe(II)FMNH2], the two irons are surrounded by four histidines, one aspartate, one glutamate and one bridging aspartate
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additional information
the reaction is not inhibited by cyanide
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additional information
the reaction is not inhibited by cyanide
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0.03
reduced coenzyme F420
0.002
O2
pH 7.6, 37°C
0.03
reduced coenzyme F420
pH 7.6, 37°C
0.03
reduced coenzyme F420
pH 7.6, 37°C
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0.4
pH 7.6, 37°C, cell suspension
55
pH 7.6, 37°C, purified enzyme
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7.5
-
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6.5 - 8.5
30% of the maximal activity at pH 6.5 and 8.5
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5.3
calculated from sequence
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UniProt
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UniProt
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SwissProt
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SwissProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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physiological function
the enzyme is involved in O2 detoxification
physiological function
the enzyme is involved in O2 detoxification
physiological function
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the enzyme is involved in O2 detoxification
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physiological function
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the enzyme is involved in O2 detoxification
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FPRA_METAZ
410
0
46060
Swiss-Prot
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FPRA_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
416
0
47380
Swiss-Prot
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FPRA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
404
0
45460
Swiss-Prot
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FPRA_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
404
0
45205
Swiss-Prot
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A0A401HR40_9EURY
409
0
46385
TrEMBL
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43000
x * 43000, SDS-PAGE
45000
x * 45000, SDS-PAGE
45300
x * 45300, calculated from sequence
46100
x * 46100, calculated from sequence
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?
x * 45000, SDS-PAGE
?
x * 46100, calculated from sequence
?
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x * 45000, SDS-PAGE
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?
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x * 46100, calculated from sequence
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?
x * 45300, calculated from sequence
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x * 43000, SDS-PAGE
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?
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x * 45300, calculated from sequence
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hanging and sitting drop vapor-diffusion method, crystal structures of F420H2 oxidase in a reduced state (2.25 A) and two oxidized states (1.7 A and 2.25 A)
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overexpression in Escherichia coli
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Seedorf, H.; Dreisbach, A.; Hedderich, R.; Shima, S.; Thauer, R.K.
F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification
Arch. Microbiol.
182
126-137
2004
Methanobrevibacter arboriphilus (B1A7S3), Methanobrevibacter arboriphilus DSM Z 744 (B1A7S3), Methanothermobacter marburgensis (Q50497), Methanothermobacter marburgensis DSM 2133 (Q50497)
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Seedorf, H.; Kahnt, J.; Pierik, A.J.; Thauer, R.K.
Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from methanogenic Archaea as determined by mass spectrometry
FEBS J.
272
5337-5342
2005
Methanothermobacter marburgensis (Q50497), Methanothermobacter marburgensis DSM 2133 (Q50497)
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Seedorf, H.; Hagemeier, C.H.; Shima, S.; Thauer, R.K.; Warkentin, E.; Ermler, U.
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic archaea catalyzing the reduction of O2 to H2O
FEBS J.
274
1588-1599
2007
Methanothermobacter marburgensis (Q50497), Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133 (Q50497)
brenda
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