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1.12.99.6: hydrogenase (acceptor)

This is an abbreviated version!
For detailed information about hydrogenase (acceptor), go to the full flat file.

Word Map on EC 1.12.99.6

Reaction

H2
+
acceptor
=
reduced acceptor

Synonyms

ECH, Ech hydrogenase, EchA, EchB, EchD, EchE, EchF, endo-hydrogenase, energy-converting hydrogenase, exo-hydrogenase, F420-reducing [NiFe] hydrogenase, factor420 hydrogenase, Fe-hydrogenase, Fe-only hydrogenase, ferredoxin hydrogenase, H2 producing hydrogenase [ambiguous], H2-sensing [NiFe] hydrogenase, Hfs, Hmd, HoxEFUYH type [NiFe] hydrogenase, HoxG, HupB, HupL, HupS, hupSLW, Hya, HyaA, HyaB, Hyb, HybA, HyC, HycE, Hyd X, Hyd-1, Hyd-2, Hyd-3, Hyd-4, HYD1, hydA, HydA1, HydA2, HydB, hydrogen dehydrogenase, hydrogen uptake hydrogenase, hydrogen-forming methylenetetrahydromethanopterin dehydrogenase, hydrogen-lyase, hydrogen-lyase [ambiguous], hydrogen:ferredoxin oxidoreductase, hydrogen:methylviologen oxidoreductase, hydrogenase (ferredoxin), hydrogenase 1, hydrogenase 2, hydrogenase 3, hydrogenase I (bidirectional), hydrogenase II, hydrogenase II (uptake), hydrogenase-1, hydrogenase-2, hydrogenase-Fe-S, hydrogenases Hyd-1, hydrogenases Hyd-2, hydrogenlyase [ambiguous], hyf, HyhL, HynSL, HynSL hydrogenase, Hyq, iron-sulfur-cluster-free hydrogenase, Mbh, membrane-bound [NiFe]-hydrogenase, methyl viologen-reducing hydrogenase, methylviologen hydrogenase, Ni-Fe hydrogenase, nickel-iron hydrogenase, NiFe hydrogenase, NiFe(Se) hydrogenase, NiFe-hydrogenase, NIFeSe-hydrogenase, regulatory hydrogenase, respiratory hydrogenase, SHI, uptake hydrogenase, uptake hydrogenase [ambiguous], uptake [NiFe] hydrogenase:, uptake [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-H2ase, [FeFe]-hydrogenase, [FeFe]H2ase, [Fe] hydrogenase, [Fe]-hydA, [Fe]-hydrogenase, [Ni-Fe] hydrogenase, [NiFeSe]-hydrogenase, [NiFe] hydrogenase, [NiFe]-hydrogenase, [NiFe]-hydrogenase 2, [NiFe]-hydrogenase-2, [NiFe]H2ase, [NiFe]hydrogenase

ECTree

     1 Oxidoreductases
         1.12 Acting on hydrogen as donor
             1.12.99 With unknown physiological acceptors
                1.12.99.6 hydrogenase (acceptor)

Purification

Purification on EC 1.12.99.6 - hydrogenase (acceptor)

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
467fold with a yield of 0.13%, to homogeneity, under anaerobic and reducing conditions using sodium dithionite as reducing agent, by ultrafiltration
-
ammonium sulfate precipitation and phenyl-Sepharose column chromatography
-
apparent homogeneity
by affinity chromatography, ca. 99% pure
-
by gel filtration, 55fold
-
by immobilized metal-affinity chromatography
-
cytosolic [NiFe] hydrogenase large subunit HyhL
DEAE 52 cellulose column chromatography
-
DEAE Sepharose column chromatography and Q Sepharose HiLoad column chromatography
-
DEAE-cellulose column chromatography and phenyl-Sepharose column chromatography
-
density-gradient centrifugation, column chromatography
-
HisTrap Ni affinity column chromatography, and Superdex 200 gel filtration
-
HydADELTAEFG purified by anion exchange chromatography
-
Ni-NTA column chromatography
-
partial
partially and fully purified
-
partially purified
Megalodesulfovibrio gigas
purification of large subunit preHoxG
-
purification of the protein under strictly anaerobic and reducing conditions to obtain the as-isolated state of HydA1
-
purified protein forms a complex with histidine protein kinase
-
Q-Sepharose column chromatography, Biogel hydroxyapatite column chromatography, and Superdex 200 gel filtration
-
recombinant enzyme
recombinant Strep-tag enzyme
Solidesulfovibrio fructosivorans
-
Strep-Tactin Superflow column chromatography
-
the large subunit HoxC is purified without its small subunit. Two forms of HoxC are identified. Both forms contain iron but only substoichiometric amounts of nickel. One form is a homodimer of HoxC whereas the second also contains the Ni-Fe site maturation proteins HypC and HypB. Despite the presence of the Ni-Fe active site in some of the proteins, both forms, which lack the Fe-S clusters normally present in hydrogenases, cannot activate hydrogen. The incomplete insertion of nickel into the Ni–Fe site provides direct evidence that Fe precedes Ni in the course of metal center assembly
-
to homogeneity by gel filtration, 2.4fold
-
to homogeneity, by gel filtration, 133fold purified and 68.2% of yield relative to the membrane
-