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H2 + coenzyme F0
reduced coenzyme F0
H2 + coenzyme F420
reduced coenzyme F420
H2 + FAD
H+ + FADH2
-
-
-
-
r
H2 + oxidized benzyl viologen
reduced benzyl viologen
H2 + oxidized coenzyme F0
reduced coenzyme F20
H2 + oxidized coenzyme F420
reduced coenzyme F420
H2 + oxidized methyl viologen
reduced methyl viologen
H2 + thioredoxin
reduced thioredoxin
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
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
-
-
?
oxidized methyl viologen + H2
reduced methyl viologen + H+
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
-
-
-
?
additional information
?
-
H2 + benzyl viologen
?
-
-
-
-
?
H2 + benzyl viologen
?
-
-
-
-
?
H2 + coenzyme F0
reduced coenzyme F0
-
-
-
?
H2 + coenzyme F0
reduced coenzyme F0
-
-
-
?
H2 + coenzyme F0
reduced coenzyme F0
-
-
-
-
?
H2 + coenzyme F0
reduced coenzyme F0
-
-
-
r
H2 + coenzyme F0
reduced coenzyme F0
-
F0 is 7,8-didemethyl-8-hydroxy-5-deazariboflavin
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
r
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
r
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
two alternative pathways, the F420-reducing hydrogenase and the Hmd-Mtd cycle (2-dependent methylenetetrahydromethanopterin dehydrogenase (Hmd) and F420H2-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) together reduce F420 with H2) can function in vivo for the reduction of F420 with H2. Furthermore, during growth on formate the same pathways function in reverse to produce H2 from F420H2. The lack of growth differences between the wild-type and mutant strains on H2 and CO2 suggests that neither pathway for F420 reduction is rate limiting. However, in nature the F420-reducing hydrogenase may constitute the major pathway when sufficient nickel is present, while the Hmd-Mtd cycle may be important when nickel is limiting
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
F420 is 7,8-didemethyl-8-hydroxy-5-deazaflavin
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
binding site for methyl viologen different from F420 binding site as determined by blocking of binding site with antibodies against native enzyme
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + methyl viologen
?
-
binding site for methyl viologen different from F420 binding site
-
-
?
H2 + methyl viologen
?
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen
-
-
-
?
H2 + oxidized coenzyme F0
reduced coenzyme F20
cofactor F0 i.e. 7,8-didemethy1-8-hydroxy-S-deazaflavin
-
-
?
H2 + oxidized coenzyme F0
reduced coenzyme F20
cofactor F0 i.e. 7,8-didemethy1-8-hydroxy-S-deazaflavin
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
?
additional information
?
-
-
generation of F420H2 by Fpo with electrons derived from DIET requires an abundance of reduced methanophenazine
-
-
-
additional information
?
-
-
reduces different flavins
-
-
?
additional information
?
-
-
reduces tetrazolium dyes with molecular oxygen
-
-
?
additional information
?
-
B6YTV8; B6YTV9; B6YTW0
the endogenous frhAGB-encoded hydrogenase does not exhibit F420-reducing activity
-
-
-
additional information
?
-
B6YTV8; B6YTV9; B6YTW0 AND
the endogenous frhAGB-encoded hydrogenase does not exhibit F420-reducing activity
-
-
-
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H2 + coenzyme F420
reduced coenzyme F420
H2 + oxidized coenzyme F420
reduced coenzyme F420
H2 + oxidized methyl viologen
reduced methyl viologen
H2 + thioredoxin
reduced thioredoxin
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
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
-
-
?
additional information
?
-
-
generation of F420H2 by Fpo with electrons derived from DIET requires an abundance of reduced methanophenazine
-
-
-
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
r
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
two alternative pathways, the F420-reducing hydrogenase and the Hmd-Mtd cycle (2-dependent methylenetetrahydromethanopterin dehydrogenase (Hmd) and F420H2-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) together reduce F420 with H2) can function in vivo for the reduction of F420 with H2. Furthermore, during growth on formate the same pathways function in reverse to produce H2 from F420H2. The lack of growth differences between the wild-type and mutant strains on H2 and CO2 suggests that neither pathway for F420 reduction is rate limiting. However, in nature the F420-reducing hydrogenase may constitute the major pathway when sufficient nickel is present, while the Hmd-Mtd cycle may be important when nickel is limiting
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
?
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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
-
loss of F420H2 dehydrogenase, and therefore of the 420H2:heterodisulfide oxidoreductase system, does not measurably affect methanogenesis or growth in Methanosarcina barkeri
metabolism
-
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
-
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
physiological function
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
-
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
additional information
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
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?
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
?
-
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
-
heterotrimer
-
-
heterotrimer
-
1 * 43000 + 1 * 31000 + 1 * 26000, SDS-PAGE
heterotrimer
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
alphabetagamma, 1 * 43000, alpha-subunit, + 1 * 30000, beta-subunit, + 1 * 25000, gamma-subunit, SDS-PAGE
hexamer
2 * 48000 (alpha) + 2 * 33000 (beta) + 2 * 30000 (gamma)
hexamer
-
2 * 48000 (alpha) + 2 * 33000 (beta) + 2 * 30000 (gamma)
-
multimer
-
alpha,beta,gamma 43600 + 36700 + 28000, SDS-PAGE, exact subunit composition not known, ratio 1:1:1 postulated
multimer
-
alpha,beta,gamma 42600 + 23500 + 35000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 42600 + 23500 + 35000, SDS-PAGE, exact subunit composition not known
-
multimer
-
alpha,beta,gamma 48000 + 32000 + 25000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 56000 + 42000 + 35000, SDS-PAGE, three subunit species found but exact subunit composition not known
multimer
-
alpha,beta,gamma,delta 55000 + 45000 + 37000 + 27000, SDS-PAGE, exact subunit composition not known, function of delta subunit not known
multimer
-
alpha,beta 5 * 50700 + 15 * 30700, SDS-PAGE, electron microscopy
multimer
alpha,beta,gamma,delta 44700 + 30700 + 25700 + 17600, calculated from DNA sequence, SDS-PAGE, delta subunit not visible in SDS-PAGE, exact subunit composition not known, function of delta subunit not known
multimer
-
alpha,beta,gamma 48000 + 33000 + 27000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 45000 + 31000 + 28000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
multimer
-
ratio alpha, beta, gamma postulated to be 1:1:1
multimer
-
alpha,beta,gamma 40000 + 31000 + 26000, SDS-PAGE, exact subunit composition not known, ratio 2:2:1 leading to MW 170000
multimer
-
alpha,beta,gamma 48000 + 33000 + 27000, SDS-PAGE, exact subunit composition not known
-
additional information
the delta subunit of hydrogenase VhuD is central to the interaction of formate dehydrogenase Fdh and heterodisulfide reductase-associated hydrogenase Vhu with heterodisulfide reductase HdrA. Under conditions where both Fdh and Vhu are expressed, these enzymes compete for binding to VhuD, which in turn binds to HdrA. Under these conditions, both enzymes are fully functional and are bound to VhuD in substoichiometric quantities. Fdh copurifies specifically with VhuD in the absence of other hydrogenase subunits
additional information
-
the delta subunit of hydrogenase VhuD is central to the interaction of formate dehydrogenase Fdh and heterodisulfide reductase-associated hydrogenase Vhu with heterodisulfide reductase HdrA. Under conditions where both Fdh and Vhu are expressed, these enzymes compete for binding to VhuD, which in turn binds to HdrA. Under these conditions, both enzymes are fully functional and are bound to VhuD in substoichiometric quantities. Fdh copurifies specifically with VhuD in the absence of other hydrogenase subunits
additional information
B6YTV8; B6YTV9; B6YTW0
enzyme peptide fingerprinting using matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS) analysis
additional information
B6YTV8; B6YTV9; B6YTW0 AND
enzyme peptide fingerprinting using matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS) analysis
additional information
B6YTV8; B6YTV9; B6YTW0
the Frh enzymes are encoded by the frhAGB genes and are heterotrimers composed of an alpha-subunit (FrhA) with a binuclear [Ni-Fe] center, a beta-subunit (FrhG) with three [4Fe-4S] clusters, and a gamma-subunit (FrhB) with one [4Fe-4S] cluster and one flavin adenine dinucleotide (FAD) as a prosthetic group
additional information
B6YTV8; B6YTV9; B6YTW0 AND
the Frh enzymes are encoded by the frhAGB genes and are heterotrimers composed of an alpha-subunit (FrhA) with a binuclear [Ni-Fe] center, a beta-subunit (FrhG) with three [4Fe-4S] clusters, and a gamma-subunit (FrhB) with one [4Fe-4S] cluster and one flavin adenine dinucleotide (FAD) as a prosthetic group
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Mukhopadhyay, B.; Purwantini, E.; Daniels, L.
Effect of methanogenic substrates on coenzyme f420-dependent N5,N10-methylene-H4MPT dehydrogenase, N5,N10-methenyl-H4MPT cyclohydrolase and F420-reducing hydrogenase activities in Methanosarcina barkeri
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Methanococcus vannielii
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Methanothermobacter thermautotrophicus
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Paramagnetic centers in the nickel-containig, deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum
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Methanothermobacter thermautotrophicus
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Two hydrogenases with distinct electron-carrier specificity and subunit composition in Methanobacterium formicicum
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Methanobacterium bryantii, Methanobacterium formicicum, Methanobacterium formicicum MF
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Nelson, M.J.K.; Brown, D.P.; Ferry, J.G.
FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum
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Methanobacterium formicicum
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1987
Methanothermobacter thermautotrophicus
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Sprott, G.D.; Shaw, K.M.; Beveridge, T.J.
Properties of the particulate enzyme F420-reducing hydrogenase isolated from Methanospirillum hungatei
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Methanothermobacter thermautotrophicus, Methanospirillum hungatei
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Muth, E.; Mrschel, E.; Klein, A.
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Methanothermobacter thermautotrophicus, Methanococcus voltae
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Baron, S.F.; Williams, D.S.; May, H.D.; Patel, P.S.; Aldrich, H.C.; Ferry, J.G.
Immunogold localization of coenzyme F420-reducing format dehydrogenase and coenzyme F420-reducing hydrogenase in Methanobacterium formicicum
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Methanobacterium formicicum
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Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum
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Methanobacterium formicicum
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Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H
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Methanothermobacter thermautotrophicus (P19496 and P19499 and P19498)
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Methanocaldococcus jannaschii
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Tachibana, A.; Tanaka, T.; Taniguchi, M.; Oi, S.
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Methanothermobacter thermautotrophicus
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Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
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Methanosarcina barkeri (P80490 and P80489 and P80491), Methanosarcina barkeri DSM 804 (P80490 and P80489 and P80491)
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Conversion of the central [4Fe-4S] cluster into a [3Fe-4S] cluster leads to reduced hydrogen-uptake activity of the F420-reducing hydrogenase of Methanococcus voltae
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Methanococcus voltae
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de Poorter, L.M.; Geerts, W.J.; Keltjens, J.T.
Hydrogen concentrations in methane-forming cells probed by the ratios of reduced and oxidized coenzyme F420
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151
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2005
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
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Surin, S.; Cubonova, L.; Majernik, A.I.; Smigan, P.
Amiloride resistance in the methanoarcheon Methanothermobacter thermoautotrophicus: characterization of membrane-associated proteins
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Methanothermobacter thermautotrophicus
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Hendrickson, E.L.; Leigh, J.A.
Roles of coenzyme F420-reducing hydrogenases and hydrogen- and F420-dependent methylenetetrahydromethanopterin dehydrogenases in reduction of F420 and production of hydrogen during methanogenesis
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Methanococcus maripaludis
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Kulkarni, G.; Kridelbaugh, D.; Guss, A.; Metcalf, W.
Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri
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2009
Methanosarcina barkeri
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Mills, D.; Vitt, S.; Strauss, M.; Shima, S.; Vonck, J.
De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy
eLife
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Methanothermobacter marburgensis (D9PYF9)
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Costa, K.C.; Lie, T.J.; Xia, Q.; Leigh, J.A.
VhuD facilitates electron flow from H2 or formate to heterodisulfide reductase in Methanococcus maripaludis
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195
5160-5165
2013
Methanococcus maripaludis (Q6LWL3), Methanococcus maripaludis
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Fiebig, K.; Friedrich, B.
Purification of the F420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)
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Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector
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3
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2014
Methanothermobacter marburgensis
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Vitt, S.; Ma, K.; Warkentin, E.; Moll, J.; Pierik, A.J.; Shima, S.; Ermler, U.
The F420-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member
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Methanothermobacter marburgensis
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Jung, H.-C.; Lim , J.K.; Yang, T.-J.; Kang, S.G.; Lee, H.S.
Direct electron transfer between the frhAGB-encoded hydrogenase and thioredoxin reductase in the nonmethanogenic archaeon Thermococcus onnurineus NA1
Appl. Environ. Microbiol.
86
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2020
Thermococcus onnurineus (B6YTV8 AND B6YTV9 AND B6YTW0), Thermococcus onnurineus (B6YTV8 AND B6YTV9 AND B6YTW0 AND)
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
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9
3109
2018
Geobacter metallireducens
brenda
Perona-Vico1, E.
Blasco-Gomez, R.; Colprim, J.; Puig, S.; Baneras, L. [NiFe]-hydrogenases are constitutively expressed in an enriched Methanobacterium sp. population during electromethanogenesis
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14
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Methanobacterium sp.
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