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Information on EC 1.12.98.1 - coenzyme F420 hydrogenase
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1.12.98.1 coenzyme F420 hydrogenaseIUBMB Comments
An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
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Word Map
- 1.12.98.1
-
methanogen
-
methanobacterium
- thermoautotrophicum
-
methanococcus
- viologens
- hydrogenases
- nife-hydrogenase
-
heterodisulfide
-
methanogenesis
-
nickel-containing
- barkeri
- voltae
- methylenetetrahydromethanopterin
- fusaro
- n5,n10-methylenetetrahydromethanopterin
-
methanothermobacter
-
si-face
-
h2-forming
- formicicum
The expected taxonomic range for this enzyme is: Euryarchaeota
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, FRH, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8-hydroxy-5-deazaflavin-reactive hydrogenase
8-hydroxy-5-deazaflavin-reducing hydrogenase
-
-
-
-
coenzyme F420-dependent hydrogenase
-
-
-
-
deazaflavin-reducing hydrogenase
-
-
-
-
EC 1.12.99.1
-
-
formerly
-
F420-reducing hydrogenase
FRH
hydrogen:(acceptor) oxidoreductase
-
-
-
-
Mbar_A0449
Mbar_A0450
Mbar_A0452
8-hydroxy-5-deazaflavin-reactive hydrogenase
-
-
F420-reducing hydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2 + oxidized coenzyme F420 = reduced coenzyme F420
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:coenzyme F420 oxidoreductase
An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
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CAS REGISTRY NUMBER
COMMENTARY
9027-05-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2 + coenzyme F0
reduced coenzyme F0
-
F0 is 7,8-didemethyl-8-hydroxy-5-deazariboflavin
-
?
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
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
Methanosarcina barkeri Fusaro / DSM 804
-
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
-
-
-
?
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
?
-
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
?
-
binding site for methyl viologen different from F420 binding site
-
-
-
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 methyl viologen
reduced methyl viologen
-
-
-
-
?
additional information
?
-
-
reduces tetrazolium dyes with molecular oxygen
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
enzyme of methanogenesis pathway
-
?
H2 + coenzyme F420
reduced coenzyme F420
Methanosarcina barkeri Fusaro / DSM 804
-
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 + 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
P80490 and P80489 and P80491
-
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
bound to protein, depleted by hydrophobic interaction chromatography
FAD
-
bound to protein, depleted by hydrophobic interaction chromatography; FAD depleted enzyme reduces methyl viologen but not F420
FAD
-
0.8-0.9 mol per mol 115000 Da species, bound to gamma subunit
FAD
-
1 mol per mol 109000 Da species; FAD depleted enzyme reduces methyl viologen but not F420
additional information
-
no activity with FMN after FAD depletion
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Nickel
selenium
sulfur
Iron
-
1 mol of the 198000 Da enzyme form contains 28-32 mol of non-heme iron
Nickel
-
Ni3+ found in aerobically purified inactive enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO
-
dead end inhibitor, competitive for H2, uncompetetitive versus F0
reduced coenzyme F0
-
noncompetitive product inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonium sulfate
-
improves reactivation of enzyme with FAD after FAD depletion
KCl
-
0.8 M activate F420-linked activity more than 10fold, slight inhibition of methyl viologen linked activity
Procion Blue HB
-
stimulates methyl viologen reduction
FAD
-
restores activity after depletion of FAD in hydrophobic interaction chromatography
FAD
-
reactivation without added FAD restores only methyl viologen-dependent activity, no activity with F420
additional information
-
2 times higher activity in biological buffers like Tris or EPPS compared with phosphate buffer
-
additional information
-
conditions for anaerobic reductive activation in the presence of hydrogen, 2-mercaptoethanol and KCl or methyl viologen yield maximal hydrogenase activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2250
coenzyme F0
-
equal turnover in reverse reaction under anaerobic conditions
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.34
-
growth with H2 and CO2, enzyme activity depends on growth substrate
0.437
-
growth on methanol, enzyme activity depends on growth substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
-
optimum pH for methyl viologen reduction above pH 11
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
-
the methylviologen-reducing activity increased with pH from pH 5.5-10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P80490: subunit beta, P80489: subunit alpha, P80491: subunit gamma
SwissProt
brenda
P80490: subunit beta, P80489: subunit alpha, P80491: subunit gamma
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to cytoplasmatic membrane and to inside-out membrane vesicles, attached to membrane by linker peptide of 10000-20000 Da
brenda
-
associated to cytoplasmatic membrane and to inside-out membrane vesicles, attached to membrane by linker peptide of 10000-20000 Da
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
in the absence of hydrogenase Vhu, growth on hydrogen still occurs, albeit slowly
Show AA Sequence and Transmembrane Helices (505 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
D9PYF7
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
30000
30700
-
alpha,beta 5 * 50700 + 15 * 30700, SDS-PAGE, electron microscopy
31000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
33000
47000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
50700
-
alpha,beta 5 * 50700 + 15 * 30700, SDS-PAGE, electron microscopy
105000
-
smallest active species, gel filtration, sucrose density centrifugation
115000
170000
198000
340000
-
gel filtration, enzyme tends to aggregate, aggregated form MW 1300000
670000
-
membrane-associated protein complex, native PAGE
790000
800000
115000
-
smallest species with enzymatic activity, native SDS-PAGE
115000
-
smallest species with enzymatic activity, native SDS-PAGE
790000
-
native SDS-PAGE, sucrose density centrifugation
800000
-
electron microscopy, shadow casting experiments, ring-shape structure found
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
hexamer
multimer
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
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
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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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
structure determined by near-atomic resolution cryo-electron microscopy with and without bound substrate F420. The 1.2-MDa complex contains 12 copies of the heterotrimer, which form a spherical protein shell with a hollow core. There is strong electron density of the chains of metal clusters running parallel to the protein shell, and the F420-binding site is located at the end of the chain near the outside of the spherical structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C205P
-
no effect on benzyl viologen reduction, 10 fold decrease in F420 reduction, wild type enzyme contains 3[4Fe-4S], mutant enzyme contains 1[3Fe-4S]
additional information
-
Methanosarcina barkeri Delta fpo mutants: strain WWM85 Delta hpt::PmcrB-Phi C31int-attP, strain WWM86 Delta hpt::PmcrB-Phi C31int-attB, strain WWM71 Delta hpt::PmcrB-Phi C31int-attB, Delta fpoA-O Deletion of fpo by markerless exchange with pDK4 in WWM86, strain WWM123 Delta hpt::PmcrB-Phi C31int-attP, Delta fpoF Deletion of fpoF by markerless exchange with pDK13 in WWM85, strain WWM116 Delta hpt::PmcrB-Phi C31int-attP, Delta freAEGB Deletion of fre by markerless exchange with pGK6 in WWM85, strain WWM122 Delta hpt::PmcrB-Phi C31int-attB, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM86, strain WWM108 Delta hpt::PmcrB-Phi C31int-attB, Delta fpoA-O, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM71, strain WWM145 Delta hpt::PmcrB-Delta C31int-attP, Delta fpoF, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM123
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
methyl viologen-reducing activity heat resistent up to 65°C, F420-reducing activity 75% inactivated at 65°C
70
-
stable for more than 3 h, methyl viologen-linked activity more stable against heating than F420-linked activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FAD stabilizes F420-linked activity against heat inactivation, generally stabilizing
-
freezing and thawing changes properties of enzyme, different behavior in anion exchange chromatography
-
unstable in prereduced buffer, dramatic decline of activity after 2 h
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic purification yields the stable but inactive enzyme, can be reactivated under reducing conditions
-
395086
extremely oxygen sensitive, can be reactivated by incubation with molecular hydrogen and dithiothreitol
-
395079
more stable under aerobic conditions, reversible loss of activity with oxygen can be restored with dithionite
-
395082
purified enzyme requires reductive reactivation before assay, reactivation possible with H2 or glucose and glucose oxidase
-
395093
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 year, inactive form maintains 70% of initial activity after reactivation
-
4°C, 4 weeks, 25% loss of activity towards F420, 97% loss of activity towards methyl viologen
-
liquid nitrogen, in presence of 50% sucrose and 10% glycerol, stable
-
room temperature, activated enzyme loses 20% of inital activity within 24 h
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
aerobic purification causes reversible inhibition with O2
-
partial
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Methanosarcina barkeri (P80490 and P80489 and P80491), Methanosarcina barkeri DSM 804 (P80490 and P80489 and P80491)
brenda
Bingemann, R.; Klein, A.
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
Eur. J. Biochem.
267
6612-6618
2000
Methanococcus voltae
brenda
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
Microbiology
151
1697-1705
2005
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
brenda
Surin, S.; Cubonova, L.; Majernik, A.I.; Smigan, P.
Amiloride resistance in the methanoarcheon Methanothermobacter thermoautotrophicus: characterization of membrane-associated proteins
Folia Microbiol. (Praha)
51
313-316
2006
Methanothermobacter thermautotrophicus
brenda
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
J. Bacteriol.
190
4818-4821
2008
Methanococcus maripaludis
brenda
Kulkarni, G.; Kridelbaugh, D.; Guss, A.; Metcalf, W.
Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri
Proc. Natl. Acad. Sci. USA
106
15915-15920
2009
Methanosarcina barkeri
brenda
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
2013
e00218
2013
Methanothermobacter marburgensis (D9PYF9)
brenda
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
J. Bacteriol.
195
5160-5165
2013
Methanococcus maripaludis, Methanococcus maripaludis (Q6LWL3)
brenda
Fiebig, K.; Friedrich, B.
Purification of the F420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)
Eur. J. Biochem.
184
79-88
1989
Methanosarcina barkeri, Methanosarcina barkeri (P80490 and P80489 and P80491), Methanosarcina barkeri DSM 804 (P80490 and P80489 and P80491)
brenda
Allegretti, M.; Mills, D.J.; McMullan, G.; Kuehlbrandt, W.; Vonck, J.
Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector
eLife
3
e01963
2014
Methanothermobacter marburgensis
brenda
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
J. Mol. Biol.
426
2813-2826
2014
Methanothermobacter marburgensis
brenda
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