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EC Tree
IUBMB Comments A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
H-II, hydrogenase II, SHI,
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SHI
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H2 + NAD(P)+ = H+ + NAD(P)H
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hydrogen:NAD(P)+ oxidoreductase
A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+).
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H+ + reduced methyl viologen
H2 + oxidized methyl viologen
H2 + NAD+
H+ + NADH
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r
H2 + NADP+
H+ + NADPH
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r
additional information
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H+ + NADPH
H2 + NADP+
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r
H+ + NADPH
H2 + NADP+
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r
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
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H+ + reduced methyl viologen
H2 + oxidized methyl viologen
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additional information
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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additional information
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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additional information
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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additional information
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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additional information
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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FAD
contains 0.83 FAD per mol enzyme
NADPH
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[2Fe-2S]-center
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contains 1 [2Fe-2S] centre
[2Fe-2S]-center
contains 1 [2Fe-2S]-center
[4Fe-4S]-center
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contains 2 [4Fe-4S] centres
[4Fe-4S]-center
contains 2 [4Fe-4S]-centers
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Fe2+
contains 21 atoms iron per mol enzyme
Iron
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contains 1 nickel-iron catalytic site and 6 iron-sulfur clusters, contains 23 iron atoms/heterotetramer
Ni2+
contains 0.9 atoms nickel per mol enzyme
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1.23
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crude native enzyme, using methyl viologen as cosubstrate, at pH 8.4 and 80°C
126
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recombinant enzyme after 24fold purification, using methyl viologen as cosubstrate, at pH 8.4 and 80°C
7.96
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crude recombinant enzyme, using methyl viologen as cosubstrate, at pH 8.4 and 80°C
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brenda
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brenda
subunit alpha
UniProt
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subunit beta
UniProt
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subunit delta
UniProt
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subunit gamma
UniProt
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brenda
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HYD2A_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
412
0
46180
Swiss-Prot
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HYD2D_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
237
0
26285
Swiss-Prot
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A0A5B9DED7_9ARCH
258
0
29419
TrEMBL
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A0A5E6MM17_9BACT
257
0
27901
TrEMBL
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A0A3B0YTX6_9ZZZZ
258
0
28774
TrEMBL
other Location (Reliability: 5 )
A0A3B1DPC7_9ZZZZ
434
0
49590
TrEMBL
other Location (Reliability: 1 )
A0A3B1CJD3_9ZZZZ
267
0
29164
TrEMBL
other Location (Reliability: 3 )
A0A1Q9N693_ODILC
Odinarchaeota archaeon (strain LCB_4)
270
0
29756
TrEMBL
-
A0A0B8NKH4_9NOCA
430
0
46880
TrEMBL
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A0A3B1DAK7_9ZZZZ
423
0
46239
TrEMBL
other Location (Reliability: 2 )
A0A3B0V3X4_9ZZZZ
433
0
48372
TrEMBL
other Location (Reliability: 1 )
A0A7G2D5H7_9EURY
415
0
46668
TrEMBL
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A0A3B1CZH9_9ZZZZ
246
0
26859
TrEMBL
other Location (Reliability: 3 )
A0A7G2D4W2_9EURY
246
0
27316
TrEMBL
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A0A3B0VIT7_9ZZZZ
268
0
29282
TrEMBL
Secretory Pathway (Reliability: 5 )
A0A1Q9NZB5_9ARCH
435
0
49469
TrEMBL
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A0A3B1A4B1_9ZZZZ
212
0
24068
TrEMBL
other Location (Reliability: 2 )
A0A380TIG0_9ZZZZ
109
0
11527
TrEMBL
other Location (Reliability: 3 )
A0A5E4HRT5_9ARCH
435
0
48945
TrEMBL
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A0A3B0QPH1_9ZZZZ
437
0
48825
TrEMBL
other Location (Reliability: 1 )
A0A3B1DRI4_9ZZZZ
34
0
3800
TrEMBL
other Location (Reliability: 2 )
A0A3B0RG25_9ZZZZ
271
0
29478
TrEMBL
other Location (Reliability: 3 )
A0A3B1CW47_9ZZZZ
246
0
26912
TrEMBL
other Location (Reliability: 3 )
A0A5E4IMA5_9ARCH
159
0
18560
TrEMBL
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HYD2B_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
334
0
39181
Swiss-Prot
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HYD2G_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
288
0
32945
Swiss-Prot
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24000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
30000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
39000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
52000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
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heterotetramer
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heterotetramer
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
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25 - 90
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the native enzyme shows half-lives of 14 h at 90°C under argon (H2 evolution), 21 h at 25°C under air (H2 evolution), and 10 h at 90°C under argon (H2 oxidation). The recombinant enzyme shows half-lives of 6 h at 90°C under argon (H2 evolution), 25 h at 25°C under air (H2 evolution), and 5 h at 90°C under argon (H2 oxidation)
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DEAE column chromatography, hydroxyapatite column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
Strep-tag II column chromatography
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synthesis
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the recombinant enzyme is efficient in vitro biohydrogen production
synthesis
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the recombinant enzyme is efficient in vitro biohydrogen production
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Ma, K.; Weiss, R.; Adams, M.W.W.
Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
J. Bacteriol.
182
1864-1871
2000
Pyrococcus furiosus, Pyrococcus furiosus (E7FHC4), Pyrococcus furiosus (E7FHF8), Pyrococcus furiosus (E7FHN9), Pyrococcus furiosus (E7FHW8)
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Chandrayan, S.K.; McTernan, P.M.; Hopkins, R.C.; Sun, J.; Jenney, F.E.; Adams, M.W.
Engineering hyperthermophilic archaeon Pyrococcus furiosus to overproduce its cytoplasmic [NiFe]-hydrogenase
J. Biol. Chem.
287
3257-3264
2012
Pyrococcus furiosus, Pyrococcus furiosus COM1
brenda
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