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Information on EC 1.5.7.2 - coenzyme F420 oxidoreductase (ferredoxin)
for references in articles please use BRENDA:EC1.5.7.2
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.7 With an iron-sulfur protein as acceptor
1.5.7.2 coenzyme F420 oxidoreductase (ferredoxin)
IUBMB Comments
The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
The expected taxonomic range for this enzyme is: Methanosarcinales
Reaction Schemes
showSynonyms
fpof protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F420H2:phenazine oxidoreductase
Fd:F420 oxidoreductase
ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit A
Fpo
FpoF protein
HdrA2
mm0627
ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit A
-
ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
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SYSTEMATIC NAME
IUBMB Comments
coenzyme F420:ferredoxin oxidoreductase
The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methanophenazine + reduced F420 + 2 H+
reduced methanophenazine + oxidized F420
-
Substrates: -
Products: -
Products: -
?
methanophenazine + reduced ferredoxin + 2 H+
reduced methanophenazine + oxidized ferredoxin
-
Substrates: -
Products: -
Products: -
?
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: -
Products: -
Products: -
?
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: -
Products: -
Products: -
?
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: -
Products: -
Products: -
r
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: FpoF can function as an ferredoxin:F420 oxidoreductase when reduced ferredoxin accumulates in the cytoplasm. As a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
Products: -
Products: -
r
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: -
Products: -
Products: -
r
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: FpoF can function as an ferredoxin:F420 oxidoreductase when reduced ferredoxin accumulates in the cytoplasm. As a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
Products: -
Products: -
r
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
Substrates: when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
Products: -
Products: -
r
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
Substrates: when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
Products: -
Products: -
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methanophenazine + reduced F420 + 2 H+
reduced methanophenazine + oxidized F420
-
Substrates: -
Products: -
Products: -
?
methanophenazine + reduced ferredoxin + 2 H+
reduced methanophenazine + oxidized ferredoxin
-
Substrates: -
Products: -
Products: -
?
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: FpoF can function as an ferredoxin:F420 oxidoreductase when reduced ferredoxin accumulates in the cytoplasm. As a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
Products: -
Products: -
r
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
Substrates: FpoF can function as an ferredoxin:F420 oxidoreductase when reduced ferredoxin accumulates in the cytoplasm. As a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
Products: -
Products: -
r
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
Substrates: when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
Products: -
Products: -
r
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
Substrates: when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
presence of two FeS clusters, 8.7 mol of nonheme iron and 5.1 mol of acid-labile sulfur per mol of protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
reduced ferredoxin
pH 7.0, temperature not specified in the publication
0.002
oxidized coenzyme F420
pH 7.0, temperature not specified in the publication
0.0064
oxidized coenzyme F420
21°C, pH not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
as a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
brenda
-
as a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
-
brenda
when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
brenda
-
when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, S° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea
evolution
-
evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, S° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea
metabolism
-
model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during coculture with Geobacter metallireducens. Each two moles of ethanol oxidized to acetate by G. metallireducens releases eight electrons and eight protons. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo. Proton translocation drives Fpo-catalyzed reduction of F420 to F420H2. Half of the F420H2 produced serves as a reductant in the carbon dioxide reduction pathway. The remaining F420H2 is the electron donor for HdrABC, which reduces ferredoxin and CoM-S-S-CoB in an electron bifurcation reaction
metabolism
-
model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during coculture with Geobacter metallireducens. Each two moles of ethanol oxidized to acetate by G. metallireducens releases eight electrons and eight protons. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo. Proton translocation drives Fpo-catalyzed reduction of F420 to F420H2. Half of the F420H2 produced serves as a reductant in the carbon dioxide reduction pathway. The remaining F420H2 is the electron donor for HdrABC, which reduces ferredoxin and CoM-S-S-CoB in an electron bifurcation reaction
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metabolism
-
model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during coculture with Geobacter metallireducens. Each two moles of ethanol oxidized to acetate by G. metallireducens releases eight electrons and eight protons. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo. Proton translocation drives Fpo-catalyzed reduction of F420 to F420H2. Half of the F420H2 produced serves as a reductant in the carbon dioxide reduction pathway. The remaining F420H2 is the electron donor for HdrABC, which reduces ferredoxin and CoM-S-S-CoB in an electron bifurcation reaction
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metabolism
Methanosarcina barkeri MS DSM 800
-
model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during coculture with Geobacter metallireducens. Each two moles of ethanol oxidized to acetate by G. metallireducens releases eight electrons and eight protons. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo. Proton translocation drives Fpo-catalyzed reduction of F420 to F420H2. Half of the F420H2 produced serves as a reductant in the carbon dioxide reduction pathway. The remaining F420H2 is the electron donor for HdrABC, which reduces ferredoxin and CoM-S-S-CoB in an electron bifurcation reaction
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physiological function
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the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420
physiological function
-
the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420. The FPO complex is mainly found in acetate-utilizing, methane-producing anaerobic Archaea where it functions to reduce the membrane-associated cofactor methanophenazine using either ferredoxin or the cytoplasmic cofactor F420
physiological function
presence of an intersubunit electron transport pathway in heterodisulfide reductase HdrA2B2C2 dependent on ferredoxin or coenzyme F420 (F420H2) as an electron donor. HdrA2B2C2 catalyzes a thermodynamically favorable, flavin-based, coupling of the endergonic one-electron reduction of ferredoxin (E0 of ca. -520 mV) with F420H2 (E0 of -380 mV) to the exergonic reduction of CoMS-SCoB (E0 of -140 mV)
physiological function
-
presence of an intersubunit electron transport pathway in heterodisulfide reductase HdrA2B2C2 dependent on ferredoxin or coenzyme F420 (F420H2) as an electron donor. HdrA2B2C2 catalyzes a thermodynamically favorable, flavin-based, coupling of the endergonic one-electron reduction of ferredoxin (E0 of ca. -520 mV) with F420H2 (E0 of -380 mV) to the exergonic reduction of CoMS-SCoB (E0 of -140 mV)
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additional information
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FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated
additional information
-
FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FPOF_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
346
0
38359
Swiss-Prot
-
HDRA2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
793
0
86918
Swiss-Prot
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic tree
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcripts for genes for most of the subunits for F420H2 dehydrogenase Fpo are higher in direct interspecies electron transfer-grown cells, i.e. in coculture with Geobacter metallireducens
transcripts for genes for most of the subunits for F420H2 dehydrogenase Fpo are higher in direct interspecies electron transfer-grown cells, i.e. in coculture with Geobacter metallireducens
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transcripts for genes for most of the subunits for F420H2 dehydrogenase Fpo are higher in direct interspecies electron transfer-grown cells, i.e. in coculture with Geobacter metallireducens
-
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transcripts for genes for most of the subunits for F420H2 dehydrogenase Fpo are higher in direct interspecies electron transfer-grown cells, i.e. in coculture with Geobacter metallireducens
-
-
transcripts for genes for most of the subunits for F420H2 dehydrogenase Fpo are higher in direct interspecies electron transfer-grown cells, i.e. in coculture with Geobacter metallireducens
Methanosarcina barkeri MS DSM 800
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q8PZ67), Methanosarcina mazei DSM 3647 (Q8PZ67)
brenda
Schut, G.; Zadvornyy, O.; Wu, C.; Peters, J.; Boyd, E.; Adams, M.
The role of geochemistry and energetics in the evolution of modern respiratory complexes from a proton-reducing ancestor
Biochim. Biophys. Acta
1857
958-970
2016
Methanosarcina mazei, Methanothrix thermoacetophila
brenda
Yan, Z.; Wang, M.; Ferry, J.G.
A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea
mBio
8
e02285-16
2017
Methanosarcina acetivorans (Q8TM02), Methanosarcina acetivorans ATCC 35395 (Q8TM02)
brenda
Holmes, D.; Rotaru, A.; Ueki, T.; Shrestha, P.; Ferry, J.; Lovley, D.
Electron and proton flux for carbon dioxide reduction in Methanosarcina barkeri during direct interspecies electron transfer
Front. Microbiol.
9
3109
2018
Methanosarcina barkeri
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.7.2)
Transporter Classification Database (TCDB): 3.D.9.1.1
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Release 2023.1 (January 2023)
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