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Literature summary extracted from

  • Germer, F.; Zebger, I.; Saggu, M.; Lendzian, F.; Schulz, R.; Appel, J.
    Overexpression, isolation and spectroscopic characterization of the bidirectional [NiFe]-hydrogenase from Synechocystis sp. PCC 6803 (2009), J. Biol. Chem., 284, 36462-36472.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.12.1.3 overexpression in Synechocystis Synechocystis sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.1.2 Iron the enzyme contains at least one [4Fe4S]+ and at least one [2Fe2S]+ cluster Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.12.1.2 H+ + NADH Synechocystis sp.
-
 H2 + NAD+
-
 ?
1.12.1.2 H+ + NADPH Synechocystis sp.
-
 H2 + NADP+
-
 ?
1.12.1.3 H2 + NADP+ Synechocystis sp.
-
 H+ + NADPH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.12.1.2 Synechocystis sp.
-
-
-
1.12.1.3 Synechocystis sp.
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.12.1.2 additional information six accessory proteins HypA-F (hydrogenase pleiotropic proteins) and one protease (HoxW) are necessary for post-translational processing of the bidirectional [NiFe] hydrogenase Synechocystis sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.1.2 Strep-Tactin-Sepharose column chromatography Synechocystis sp.
1.12.1.3 single affinity chromatography, 4°C, aerobic conditions Synechocystis sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.12.1.2 0.076
-
 crude extract, pH and temperature not specified in the publication Synechocystis sp.
1.12.1.2 87.78
-
 after 1155old purification, pH and temperature not specified in the publication Synechocystis sp.
1.12.1.3 0.076
-
 crude extract Synechocystis sp.
1.12.1.3 87.78
-
 after affinity chromatogrphy Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.1.2 H+ + NADH
-
 Synechocystis sp. H2 + NAD+
-
 ?
1.12.1.2 H+ + NADPH
-
 Synechocystis sp. H2 + NADP+
-
 ?
1.12.1.2 H+ + reduced dithionite
-
 Synechocystis sp. H2 + oxidized dithionite
-
 ?
1.12.1.2 H+ + reduced methyl viologen
-
 Synechocystis sp. H2 + oxidized methyl viologen
-
 ?
1.12.1.3 H2 + NADP+
-
 Synechocystis sp. H+ + NADPH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.12.1.3 pentamer 16.5% tricine-SDS Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.12.1.2 bidirectional [NiFe] hydrogenase
-
 Synechocystis sp.
1.12.1.2 Hox
-
 Synechocystis sp.
1.12.1.3 NiFe-hydrogenase
-
 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.1.2 NADH
-
 Synechocystis sp.
1.12.1.2 NADPH
-
 Synechocystis sp.