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H2 + coenzyme F0
reduced coenzyme F0
H2 + coenzyme F420
reduced coenzyme F420
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
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
P19496 and P19499 and P19498
-
-
?
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
P19496 and P19499 and P19498
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
?
-
-
-
-
?
H2 + methyl viologen
?
-
binding site for methyl viologen different from F420 binding site
-
-
-
H2 + methyl viologen
?
-
-
-
-
?
H2 + oxidized benzyl viologen

reduced benzyl viologen
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F0

reduced coenzyme F20
P80490 and P80489 and P80491
cofactor F0 i.e. 7,8-didemethy1-8-hydroxy-S-deazaflavin
-
-
?
H2 + oxidized coenzyme F0
reduced coenzyme F20
P80490 and P80489 and P80491
cofactor F0 i.e. 7,8-didemethy1-8-hydroxy-S-deazaflavin
-
-
?
H2 + oxidized coenzyme F420

reduced coenzyme F420
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized methyl viologen

reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
-
?
additional information

?
-
-
reduces different flavins
-
-
-
additional information
?
-
-
reduces tetrazolium dyes with molecular oxygen
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
H2 + coenzyme F420
reduced coenzyme F420
H2 + oxidized coenzyme F420
reduced coenzyme F420
H2 + oxidized methyl viologen
reduced methyl viologen
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
P19496 and P19499 and P19498
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
-
enzyme of methanogenesis pathway
-
?
H2 + oxidized coenzyme F420

reduced coenzyme F420
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized methyl viologen

reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
-
?
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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
?

-
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
?
-
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
-
heterotrimer

-
1 * 43000 + 1 * 31000 + 1 * 26000, 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 42600 + 23500 + 35000, SDS-PAGE, exact subunit composition not known
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 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 40000 + 31000 + 26000, SDS-PAGE, exact subunit composition not known, ratio 2:2:1 leading to MW 170000
multimer
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
multimer
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE; ratio alpha, beta, gamma postulated to be 1:1:1
multimer
-
alpha,beta,gamma 45000 + 31000 + 28000, SDS-PAGE, exact subunit composition not known
multimer
P19496 and P19499 and P19498
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 48000 + 33000 + 27000, SDS-PAGE, exact subunit composition not known
-
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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
Arch. Microbiol.
159
141-146
1993
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
-
brenda
Yamazaki, S.
A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue
J. Biol. Chem.
257
7926-7929
1982
Methanococcus vannielii
brenda
Jacobson, F.S.; Daniels, L.; Fox, J.A.; Walsh, C.T.; Orme-Johnson, W.H.
Purification and properties of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum
J. Biol. Chem.
257
3385-3388
1982
Methanothermobacter thermautotrophicus
brenda
Kojima, N.; Fox, J.A.; Hausinger, R.P.; Daniels, L.; Orme-Johnson, W.H.; Walsh, C.
Paramagnetic centers in the nickel-containig, deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum
Proc. Natl. Acad. Sci. USA
80
378-382
1983
Methanothermobacter thermautotrophicus
brenda
Jin, S.L.C.; Blanchard, D.K.; Chen, J.S.
Two hydrogenases with distinct electron-carrier specificity and subunit composition in Methanobacterium formicicum
Biochim. Biophys. Acta
748
8-20
1983
Methanobacterium bryantii, Methanobacterium formicicum, Methanobacterium formicicum MF
-
brenda
Nelson, M.J.K.; Brown, D.P.; Ferry, J.G.
FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum
Biochem. Biophys. Res. Commun.
120
775-781
1984
Methanobacterium formicicum
brenda
Wackett, L.P.; Hartwieg, E.A.; King, J.A.; Orme-Johnson, W.H.; Walsh, C.T.
Electron microscopy of nickel-containing methanogenic enzymes: methyl reductase and F420-reducing hydrogenase
J. Bacteriol.
169
718-727
1987
Methanothermobacter thermautotrophicus
brenda
Baron, S.F.; Brown, D.P.; Ferry, J.G.
Locations of the hydrogenases of Methanobacterium formicicum after subcellular fractionation of cell extract
J. Bacteriol.
169
3823-3825
1987
Methanobacterium formicicum
brenda
Fox, J.A.; Livingston, D.J.; Orme-Johnson, W.H.; Walsh, C.T.
8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization
Biochemistry
26
4219-4227
1987
Methanothermobacter thermautotrophicus
brenda
Sprott, G.D.; Shaw, K.M.; Beveridge, T.J.
Properties of the particulate enzyme F420-reducing hydrogenase isolated from Methanospirillum hungatei
Can. J. Microbiol.
33
896-904
1987
Methanospirillum hungatei, Methanothermobacter thermautotrophicus
-
brenda
Muth, E.; Mörschel, E.; Klein, A.
Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae
Eur. J. Biochem.
169
571-577
1987
Methanococcus voltae
brenda
Livingston, D.J.; Fox, J.A.; Orme-Johnson, W.H.; Walsh, C.T.
8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 2. Kinetic and hydrogen-transfer studies
Biochemistry
26
4228-4237
1987
Methanococcus voltae, Methanothermobacter thermautotrophicus
brenda
Muth, E.
Localization of the F420-reducing hydrogenase in Methanococcus voltae cells by immuno-gold technique
Arch. Microbiol.
150
205-207
1988
Methanococcus voltae
-
brenda
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
Arch. Microbiol.
151
307-313
1989
Methanobacterium formicicum
-
brenda
Baron, S.F.; Ferry, J.G.
Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum
J. Bacteriol.
171
3846-3853
1989
Methanobacterium formicicum
brenda
Alex, L.A.; Reeve, J.N.; Orme-Johnson, W.H.; Walsh, C.T.
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
Biochemistry
29
7237-7244
1990
Methanothermobacter thermautotrophicus (P19496 and P19499 and P19498)
brenda
Shah, N.N.; Clark, D.S.
Partial purification and characterization of two hydrogenases from the extreme thermophile Methanococcus jannaschii
Appl. Environ. Microbiol.
56
858-863
1990
Methanocaldococcus jannaschii
brenda
Tachibana, A.; Tanaka, T.; Taniguchi, M.; Oi, S.
Some properties of F420-reducing hydrogenase of Methanobacterium thermoformicicum strain SF-4
Biosci. Biotechnol. Biochem.
57
156-157
1993
Methanothermobacter thermautotrophicus
brenda
Braks, I.J.; Hoppert, M.; Roge, S.; Mayer, F.
Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg
J. Bacteriol.
176
7677-7687
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Michel, R.; Massanz, C.; Kostka, S.; Richter, M.; Fiebig, K.
Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro
Eur. J. Biochem.
233
727-735
1995
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