BRENDA - Enzyme Database
show all sequences of 1.12.7.2

Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction

Ma, K.; Weiss, R.; Adams, M.W.W.; J. Bacteriol. 182, 1864-1871 (2000)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADP+
-
Pyrococcus furiosus
0.07
-
NADH
-
Pyrococcus furiosus
0.07
-
NADPH
-
Pyrococcus furiosus
0.125
-
NAD+
-
Pyrococcus furiosus
0.2
-
sulfur
-
Pyrococcus furiosus
1
-
methyl viologen
at 120 kPa H2
Pyrococcus furiosus
1.25
-
reduced methyl viologen
-
Pyrococcus furiosus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Pyrococcus furiosus
5737
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
21 atoms per mol heterotetramer; five [4Fe4S] clusters, 2 in the beta subunit and 3 in the delta subunit, additionally one [2Fe2S] cluster in the gamma subunit
Pyrococcus furiosus
Ni
0.9 atoms per mol heterotetramer, NiFe-catalytic site in the alpha-subunit
Pyrococcus furiosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
24000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
30000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
39000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
52000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
320000
-
gel filtration
Pyrococcus furiosus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus furiosus
-
hydrogenase II; strain DSM 3638
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.02
-
hydrogen production, oxidized ferredoxin as electron donor, hydrogenase II
Pyrococcus furiosus
0.2
-
sulfur reduction, hydrogenase II
Pyrococcus furiosus
0.98
-
hydrogen production, sodium dithionite as electron donor, hydrogenase II
Pyrococcus furiosus
11
-
hydrogen oxidation, methyl viologen as electron acceptor, hydrogenase II
Pyrococcus furiosus
40
-
hydrogen production, methyl viologen as electron donor, hydrogenase II
Pyrococcus furiosus
131
-
hydrogen oxidation, benzyl viologen as electron acceptor, hydrogenase II
Pyrococcus furiosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
H+ + reduced methyl viologen
-
439641
Pyrococcus furiosus
H2 + oxidized methyl viologen
-
-
-
-
H2 + electron acceptor
methyl viologen as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
H2 + electron acceptor
benzyl viologen as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
H2 + electron acceptor
NADP+ as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
additional information
ferredoxin is not an efficient electron carrier for both hydrogenases
439641
Pyrococcus furiosus
?
-
-
-
-
S + NADPH
-
439641
Pyrococcus furiosus
H2S + NADP+
-
439641
Pyrococcus furiosus
?
Subunits
Subunits
Commentary
Organism
octamer
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
above 90°C, hydrogenase II
Pyrococcus furiosus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
95
-
50% inactivation after 6 h, hydrogenase II
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
hydrogenase II, 0.83 mol per mol heterotetramer; putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
NADH
putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
NADPH
putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
hydrogenase II, 0.83 mol per mol heterotetramer; putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
NADH
putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
NADPH
putative nucleotide-binding site in the gamma subunit
Pyrococcus furiosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADP+
-
Pyrococcus furiosus
0.07
-
NADH
-
Pyrococcus furiosus
0.07
-
NADPH
-
Pyrococcus furiosus
0.125
-
NAD+
-
Pyrococcus furiosus
0.2
-
sulfur
-
Pyrococcus furiosus
1
-
methyl viologen
at 120 kPa H2
Pyrococcus furiosus
1.25
-
reduced methyl viologen
-
Pyrococcus furiosus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Pyrococcus furiosus
5737
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
21 atoms per mol heterotetramer; five [4Fe4S] clusters, 2 in the beta subunit and 3 in the delta subunit, additionally one [2Fe2S] cluster in the gamma subunit
Pyrococcus furiosus
Ni
0.9 atoms per mol heterotetramer, NiFe-catalytic site in the alpha-subunit
Pyrococcus furiosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
24000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
30000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
39000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
52000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
320000
-
gel filtration
Pyrococcus furiosus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.02
-
hydrogen production, oxidized ferredoxin as electron donor, hydrogenase II
Pyrococcus furiosus
0.2
-
sulfur reduction, hydrogenase II
Pyrococcus furiosus
0.98
-
hydrogen production, sodium dithionite as electron donor, hydrogenase II
Pyrococcus furiosus
11
-
hydrogen oxidation, methyl viologen as electron acceptor, hydrogenase II
Pyrococcus furiosus
40
-
hydrogen production, methyl viologen as electron donor, hydrogenase II
Pyrococcus furiosus
131
-
hydrogen oxidation, benzyl viologen as electron acceptor, hydrogenase II
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
H+ + reduced methyl viologen
-
439641
Pyrococcus furiosus
H2 + oxidized methyl viologen
-
-
-
-
H2 + electron acceptor
methyl viologen as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
H2 + electron acceptor
benzyl viologen as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
H2 + electron acceptor
NADP+ as electron acceptor
439641
Pyrococcus furiosus
H+ + reduced electron acceptor
-
-
-
r
additional information
ferredoxin is not an efficient electron carrier for both hydrogenases
439641
Pyrococcus furiosus
?
-
-
-
-
S + NADPH
-
439641
Pyrococcus furiosus
H2S + NADP+
-
439641
Pyrococcus furiosus
?
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
above 90°C, hydrogenase II
Pyrococcus furiosus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
95
-
50% inactivation after 6 h, hydrogenase II
Pyrococcus furiosus
Other publictions for EC 1.12.7.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Engineering the respiratory me ...
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1
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4
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1
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1
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1
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6
1
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742784
Zheng
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196
3840-3852
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-
-
-
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-
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1
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4
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1
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742859
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Intact functional fourteen-su ...
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289
19364-19372
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-
-
-
-
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1
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1
2
-
5
-
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1
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4
1
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1
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1
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1
2
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1
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4
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
726335
Ghysels
Function of the chloroplast hy ...
Chlamydomonas reinhardtii
PLoS ONE
8
e64161
2013
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2
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6
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1
1
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-
724909
Silakov
-
Unraveling the electronic prop ...
Desulfovibrio desulfuricans
Eur. J. Inorg. Chem.
2011
1056-1066
2011
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712301
Major
Characterization of energy-con ...
Methanococcus maripaludis
J. Bacteriol.
192
4022-4030
2010
-
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-
1
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2
1
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2
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1
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1
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2
1
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2
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-
1
1
-
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712307
Welte
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Methanosarcina mazei
J. Bacteriol.
192
674-678
2010
-
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1
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1
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1
1
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1
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1
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1
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1
1
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1
1
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727467
Welte
Involvement of Ech hydrogenase ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
FEBS J.
277
3396-3403
2010
-
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2
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6
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4
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4
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1
1
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701537
Marques
Purification, crystallization ...
Desulfovibrio vulgaris
Acta Crystallogr. Sect. F
65
920-922
2009
-
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1
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2
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2
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1
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1
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1
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704088
Dutta
-
Purification and characterizat ...
Enterobacter cloacae
Int. J. Hydrogen Energy
34
7530-7537
2009
-
-
-
-
-
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-
2
1
1
2
-
-
1
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1
-
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-
2
-
4
1
1
1
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1
1
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1
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2
1
1
2
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1
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2
-
4
1
1
1
-
-
1
1
-
1
-
-
-
-
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705334
Long
Hydrogenase/ferredoxin charge- ...
Chlamydomonas reinhardtii
J. Phys. Chem. A
113
4060-4067
2009
-
-
-
-
6
-
-
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2
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1
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1
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1
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6
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1
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711817
Stripp
How algae produce hydrogen--ne ...
Chlamydomonas moewusii, Chlamydomonas reinhardtii, Chlorella fusca, Chlorococcum submarinum, Clostridium acetobutylicum, Clostridium pasteurianum, Desulfovibrio desulfuricans, Megasphaera elsdenii, Tetradesmus obliquus
Dalton Trans.
2009
9960-9969
2009
-
-
-
-
-
-
-
-
-
9
12
9
-
12
-
-
1
-
-
-
-
-
10
1
-
-
-
-
-
-
-
9
-
-
-
-
-
-
9
-
-
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-
9
12
9
-
-
-
1
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-
10
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
712281
Schut
The iron-hydrogenase of Thermo ...
Thermotoga maritima
J. Bacteriol.
191
4451-4457
2009
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1
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4
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1
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2
1
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684643
Akhtar
Deletion of iscR stimulates re ...
Clostridium acetobutylicum
Appl. Microbiol. Biotechnol.
78
853-862
2008
-
-
1
-
-
-
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Hydrogenases and hydrogen phot ...
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2
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2
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Complete activity profile of C ...
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1
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Forzi
Assignment of the [4Fe-4S] clu ...
Methanosarcina barkeri
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675496
Hedderich
Energy-converting [NiFe] hydro ...
Caldanaerobacter subterraneus subsp. tengcongensis, Carboxydothermus hydrogenoformans, Escherichia coli, Methanosarcina barkeri, Pyrococcus furiosus, Rhodospirillum rubrum
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12
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6
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12
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656734
Soboh
A multisubunit membrane-bound ...
Caldanaerobacter subterraneus subsp. tengcongensis
Microbiology
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2004
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659110
Hedderich
Energy-converting [NiFe] hydro ...
Caldanaerobacter subterraneus subsp. tengcongensis, Methanosarcina barkeri, Pyrococcus furiosus
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2004
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1
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660222
Semin
Accumulation of ferrous iron i ...
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2003
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Florin
A novel type of iron hydrogena ...
Tetradesmus obliquus
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2001
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1
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1
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4
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1
1
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439651
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Mossbauer characterization of ...
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439641
Ma
Characterization of hydrogenas ...
Pyrococcus furiosus
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1864-1871
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3
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2
2
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6
-
6
1
1
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1
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439652
Sapra
Purification and characterizat ...
Pyrococcus furiosus
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182
3423-3428
2000
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1
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1
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2
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1
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1
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2
2
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1
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1
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2
-
4
1
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1
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722171
Silva
Enzymes of hydrogen metabolism ...
Pyrococcus furiosus
Eur. J. Biochem.
267
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2000
1
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3
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3
-
1
3
-
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439643
Meuer
Purification and catalytic pro ...
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
Eur. J. Biochem.
265
325-335
1999
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1
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1
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1
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5
-
7
-
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439654
Ueno
Purification and characterizat ...
Alvikia littoralis
FEBS Lett.
443
144-148
1999
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1
2
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1
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1
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1
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1
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1
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2
1
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1
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1
-
1
-
1
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-
1
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-
-
-
-
-
-
-
-
439656
Garcin
The crystal structure of a red ...
Desulfomicrobium baculatum
Structure
7
557-566
1999
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2
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1
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439638
Fontecilla-Camps
Hydrogenase: a hydrogen-metabo ...
Desulfovibrio gigas
Biochimie
79
661-666
1997
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-
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2
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2
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1
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-
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-
-
-
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439657
Romao
Characterization of the [NiFe] ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough ATCC 29579
Biochem. Biophys. Res. Commun.
240
75-79
1997
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2
2
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1
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1
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2
2
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1
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2
-
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1
-
-
-
-
-
-
-
-
-
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439659
Dobrindt
Purification and characterizat ...
Sporomusa sphaeroides
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165
141-147
1996
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-
-
-
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1
3
2
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3
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1
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1
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3
1
1
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1
1
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-
-
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1
3
2
4
-
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1
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-
1
-
3
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
439660
Fischer
Purification and characterizat ...
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans ATC 19859
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165
289-296
1996
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3
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8
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1
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1
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4
1
1
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1
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2
3
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1
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-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
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439661
Yanke
Hydrogenase I of Clostridium p ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Anaerobe
1
61-67
1995
-
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-
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2
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12
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2
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4
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2
-
4
-
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-
-
-
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-
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439663
Kemner
-
Purification and characterizat ...
Methanosarcina barkeri, Methanosarcina barkeri MS / DSM 800
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161
47-54
1994
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1
1
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3
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2
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1
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5
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10
1
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1
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1
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2
3
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1
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5
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10
1
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439664
Ma
Hydrogenase of the hyperthermo ...
Pyrococcus furiosus
Proc. Natl. Acad. Sci. USA
90
5341-5344
1993
1
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1
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1
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1
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2
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2
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439665
Happe
Isolation, characterization an ...
Chlamydomonas reinhardtii 137 C(+), Chlamydomonas reinhardtii
Eur. J. Biochem.
214
475-481
1993
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2
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1
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1
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6
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1
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1
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2
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1
1
2
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1
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1
2
6
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1
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439632
Bryant
Characterization of hydrogenas ...
Pyrococcus furiosus
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1989
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1
1
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1
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1
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2
4
1
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1
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3
1
1
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1
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439667
George
X-ray-absorption-spectroscopic ...
Clostridium pasteurianum
Biochem. J.
259
597-600
1989
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1
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439668
Macor
An investigation of hydrogenas ...
Clostridium pasteurianum
J. Biol. Chem.
262
9945-9947
1987
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439669
Adams
The physical and catalytic pro ...
Clostridium pasteurianum, Clostridium pasteurianum W5
J. Biol. Chem.
259
7045-7055
1984
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6
8
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11
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6
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6
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439670
Adams
-
The purification of hydrogenas ...
Clostridium pasteurianum
Biochim. Biophys. Acta
766
51-61
1984
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439671
Chen
Purification and properties of ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Biochem. Biophys. Res. Commun.
122
9-16
1984
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12
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10
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439672
Roessler
Purification of hydrogenase fr ...
Chlamydomonas reinhardtii 137 C(+), Chlamydomonas reinhardtii
Plant Physiol.
75
705-709
1984
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2
2
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5
1
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6
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1
6
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439673
Schneider
Purification of hydrogenases b ...
Clostridium pasteurianum, Clostridium pasteurianum MR 505, Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Biochem. J.
213
391-398
1983
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46
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439674
Van Dijk
The effects of pH and redox po ...
Megasphaera elsdenii
Eur. J. Biochem.
114
209-219
1981
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439675
Khan
The effect of electron carrier ...
Clostridium pasteurianum
Biochim. Biophys. Acta
659
457-465
1981
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1
1
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439676
Van Dijk
Properties of the hydrogenase ...
Megasphaera elsdenii
Eur. J. Biochem.
107
251-261
1980
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6
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1
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439677
Van Dijk
Purification and properties of ...
Megasphaera elsdenii, Megasphaera elsdenii LC1
Eur. J. Biochem.
102
317-330
1979
3
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439678
Klibanov
Chelating agents protect hydro ...
Clostridium pasteurianum
Biochim. Biophys. Acta
547
411-416
1979
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439679
Chen
Isolation and properties of a ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Biochem. Biophys. Res. Commun.
84
1144-1150
1978
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11
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439680
Klibanov
A rationale for stabilization ...
Clostridium pasteurianum
Proc. Natl. Acad. Sci. USA
75
3640-3643
1978
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1
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439681
Erbes
The kinetics of methyl viologe ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Biochim. Biophys. Acta
525
45-54
1978
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11
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8
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439682
Chen
Purification and properties of ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Biochim. Biophys. Acta
371
283-298
1974
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2
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1
2
2
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10
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1
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8
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1
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8
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439683
Thauer
The reaction of the iron-sulfu ...
Clostridium pasteurianum
Eur. J. Biochem.
42
447-452
1974
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1
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439684
Nakos
Structural properties of hydro ...
Clostridium pasteurianum, Clostridium pasteurianum W5
Biochemistry
10
2442-2449
1971
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1
1
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10
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1
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4
1
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