1.12.98.1: coenzyme F420 hydrogenase
This is an abbreviated version!
For detailed information about coenzyme F420 hydrogenase, go to the full flat file.
Word Map on EC 1.12.98.1
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1.12.98.1
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methanogen
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methanobacterium
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thermoautotrophicum
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methanococcus
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hydrogenases
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nife-hydrogenase
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viologens
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methanogenesis
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heterodisulfide
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nickel-containing
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barkeri
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voltae
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fusaro
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si-face
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methanothermobacter
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n5,n10-methylenetetrahydromethanopterin
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formicicum
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methylenetetrahydromethanopterin
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hydrogen-dependent
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h2-forming
- 1.12.98.1
-
methanogen
- methanobacterium
- thermoautotrophicum
-
methanococcus
- hydrogenases
- nife-hydrogenase
- viologens
-
methanogenesis
-
heterodisulfide
-
nickel-containing
- barkeri
- voltae
- fusaro
-
si-face
-
methanothermobacter
- n5,n10-methylenetetrahydromethanopterin
- formicicum
- methylenetetrahydromethanopterin
-
hydrogen-dependent
-
h2-forming
Reaction
Synonyms
8-hydroxy-5-deazaflavin-reactive hydrogenase, 8-hydroxy-5-deazaflavin-reducing hydrogenase, coenzyme F420-dependent hydrogenase, coenzyme F420-reducing dehydrogenase, deazaflavin-reducing hydrogenase, EC 1.12.99.1, F420-reducing hydrogenase, F420-reducing [NiFe] hydrogenase, F420-reducing [NiFe]-hydrogenase, F420H2 dehydrogenase, Fpo, FRH, FrhABC, FrhABG, frhAGB-encoded hydrogenase, hydrogen:(acceptor) oxidoreductase, Mbar_A0449, Mbar_A0450, Mbar_A0452, TON_1559, TON_1560, TON_1561, VhuD
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General Information
General Information on EC 1.12.98.1 - coenzyme F420 hydrogenase
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evolution
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
the F420-binding motif of the frhB-encoded subunit is not well conserved
malfunction
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loss of F420H2 dehydrogenase, and therefore of the 420H2:heterodisulfide oxidoreductase system, does not measurably affect methanogenesis or growth in Methanosarcina barkeri
metabolism
physiological function
additional information
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the preferred electron transport chain involves production of hydrogen gas in the cytoplasm, which then diffuses out of the cell, where it is reoxidized with transfer of electrons into the energy-conserving electron transport chain. This hydrogen-cycling metabolism leads directly to production of a proton motive force that can be used by the cell for ATP synthesis
metabolism
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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. Fpo plays a key role in electron transport for carbon dioxide reduction to methane during direct interspecies electron transfer (DIET)
metabolism
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to thioredoxin reductase (TrxR) and reduce Pdo, a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Functionality of the frhAGB-encoded hydrogenase utilizing a protein as an electron acceptor
metabolism
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
in general, F420-reducing hydrogenases (Frh) are key enzymes in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-H4MPT dehydrogenase and the methylene-H4MPT reductase reactions. Redox cascade from the frhAGB-encoded hydrogenase to Pdo via TrxR
in the absence of hydrogenase Vhu, growth on hydrogen still occurs, albeit slowly
physiological function
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
in the hyperthermophilic archaeon Thermococcus onnurineus strain NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR EC 1.8.1.9). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo, a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NAD(P)H in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologues, F420-reducing hydrogenases of methanogens. F420-reducing hydrogenase (Frh) is a key enzyme in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-H4MPT dehydrogenase and the methylene-H4MPT reductase reactions
physiological function
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
key enzyme in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-tetrahydromethanopterin dehydrogenase and the methylene-tetrahydromethanopterin reductase reactions
physiological function
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the external proton gradient necessary to drive the otherwise thermodynamically unfavorable reverse electron transport for F420H2 dehydrogenase (Fpo)-catalyzed F420 reduction (in Methanosarcina barkeri) is derived from protons released from Geobacter metallireducens metabolism. Enzyme Fpo plays a key role in electron transport for carbon dioxide reduction to methane during direct interspecies electron transfer (DIET). During methylotrophic methanogenesis in Methanosarcina barkeri, Fpo oxidizes F420H2 with the reduction of methanophenazine in the membrane, coupled with vectorial proton translocation to the outside of the membrane. Under some conditions Fpo may catalyze the reverse reaction in which reduced methanophenazine serves as the electron donor for the reduction of F420. In this direction, proton translocation through Fpo into the cytoplasm is required in order to make the reaction thermodynamically favorable. The Fpo-catalyzed reduction of F420 is proton balanced
B6YTV8; B6YTV9; B6YTW0
thioredoxin reductase (EC 1.8.1.9) TrxR might interact with the FrhA or FrhG subunit in the absence of the FrhB subunit
additional information
B6YTV8; B6YTV9; B6YTW0 AND
thioredoxin reductase (EC 1.8.1.9) TrxR might interact with the FrhA or FrhG subunit in the absence of the FrhB subunit