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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)

Crystallization

Crystallization on EC 1.12.99.6 - hydrogenase (acceptor)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
to 1.5 A resolution. The heterodimeric enzyme consists of a large subunit harbouring the catalytic centre in the H2-reduced state and a small subunit containing an electron relay consisting of three different iron-sulfur clusters. The cluster proximal to the active site displays an unprecedented [4Fe-3S] structure and is coordinated by six cysteines. According to the current model, this cofactor operates as an electronic switch depending on the nature of the gas molecule approaching the active site. It serves as an electron acceptor in the course of H2 oxidation and as an electron-delivering device upon O2 attack at the active site
sitting drop vapor diffusion method
-
[NiFe] hydrogenase has two different oxidized states, Ni-A (unready, exhibits a lag phase in reductive activation) and Ni-B (ready). Conversion of Ni-B to Ni-A with the use of Na2S and O2 and determination of the high-resolution crystal structures of both states
-
sitting drop vapor diffusion technique, the crystal structure of recombinant enzyme is solved to a maximum resolution of 1.5 A (reduced) or 2.2 A (as-isolated)
to 3.3 A resolution, in a 2:1 complex with its physiological partner, cytochrome b. From the short distance between distal [Fe4S4] clusters, a rapid transfer of H2-derived electrons between hydrogenase heterodimers is predicted. Thus, under low O2 levels, a functional active site in one heterodimer can reductively reactivate its O2-exposed counterpart in the other
hanging drop vapor diffusion method
Megalodesulfovibrio gigas
-
in complex with an iron guanylyl pyridone,
-
mutant C176A crystallized in the presence of dithiothreitol, at 1.95 A resolution
-