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Literature summary extracted from

  • Wang, S.; Huang, H.; Kahnt, J.; Thauer, R.K.
    A reversible electron-bifurcating ferredoxin- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica (2013), J. Bacteriol., 195, 1267-1275.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.12.1.4 additional information
-
 H2 apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C Moorella thermoacetica
1.12.1.4 0.2
-
 NAD+ pH 7.5, 45°C Moorella thermoacetica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.1.4 Iron purified enzyme contains 31 irons and 0.8 FMN per heterotrimer Moorella thermoacetica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.12.1.4 17000
-
-
 Moorella thermoacetica
1.12.1.4 63000
-
-
 Moorella thermoacetica
1.12.1.4 67000
-
-
 Moorella thermoacetica
1.12.1.4 300000
-
 gel filtration Moorella thermoacetica

Organism

EC Number Organism UniProt Comment Textmining
1.12.1.4 Moorella thermoacetica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.1.4 under strictly anoxic conditions, the enzyme is inactivated in the presence of even trace amounts of O2 Moorella thermoacetica

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.12.1.4 4.6
-
 oxidation of ferredoxin, pH 7.5, 45°C Moorella thermoacetica
1.12.1.4 57.5
-
 reduction of ferredoxin, pH 7.5, 45°C Moorella thermoacetica
1.12.1.4 195
-
 reduction of methyl viologen, pH 7.5, 45°C Moorella thermoacetica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.1.4 NAD+ + 2 oxidized ferredoxin + 2 H2
-
 Moorella thermoacetica NADH + 3 H+ + 2 reduced ferredoxin ferredoxin reduction with H2 is driven by the exergonic reduction of NAD+ (E0 -320 mV) with H2. In the absence of NAD+, ferredoxin is not reduced ?
1.12.1.4 NAD+ + 2 oxidized methyl viologen + 2 H2
-
 Moorella thermoacetica NADH + 3 H+ + 2 reduced methyl viologen
-
 ?
1.12.1.4 NADH + 3 H+ + 2 reduced ferredoxin
-
 Moorella thermoacetica NAD+ + 2 oxidized ferredoxin + 2 H2 per mol NADH, about 2 mol H2 is formed ?
1.12.1.4 NADH + 3 H+ + 2 reduced methyl viologen
-
 Moorella thermoacetica NAD+ + 2 oxidized methyl viologen + 2 H2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.12.1.4 heterohexamer 2 * 67000, subunit HydB, plus 2 * 63000, subunit HydA, plus 2 * 17000, subunit HydC, SDS-PAGE Moorella thermoacetica

Synonyms

EC Number Synonyms Comment Organism
1.12.1.4 electron-bifurcating ferredoxin- and NAD-dependent hydrogenase
-
 Moorella thermoacetica
1.12.1.4 HydABC
-
 Moorella thermoacetica

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.1.4 FMN purified enzyme contains 31 irons and 0.8 FMN per heterotrimer Moorella thermoacetica
1.12.1.4 iron-sulfur centre subunit HydA (63 kDa) is predicted to harbor the H cluster, i.e., the [6Fe4S] hydrogenase active site, three [4Fe4S] clusters, and one [2Fe2S] cluster. Subunit HydB (67 kDa) is predicted to harbor three [4Fe4S] clusters, a flavin binding site, and an NAD binding site. HydC (17 kDa) is predicted to harbor one [2Fe2S] cluster Moorella thermoacetica
1.12.1.4 NAD+
-
 Moorella thermoacetica
1.12.1.4 NADH
-
 Moorella thermoacetica