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• W2034985989 abstract "Moorella thermoacetica was long the only model organism used to study the biochemistry of acetogenesis from CO2. Depending on the growth substrate, this Gram-positive bacterium can either form H2 or consume it. Despite the importance of H2 in its metabolism, a hydrogenase from the organism has not yet been characterized. We report here the purification and properties of an electron-bifurcating [FeFe]-hydrogenase from M. thermoacetica and show that the cytoplasmic enzyme efficiently catalyzes both H2 formation and H2 uptake. The purified heterotrimeric iron-sulfur flavoprotein (HydABC) catalyzed the coupled reduction of ferredoxin (Fd) and NAD+ with H2 at 55°C at pH 7.5 at a specific rate of about 100 μmol min−1 mg protein−1 and the reverse reaction, the coupled reduction of protons to H2 with reduced ferredoxin and NADH, at a specific rate of about 10 μmol min−1 mg protein−1 in the stoichiometry Fdox + NAD+ + 2H2 ⇋ Fdred2− + NADH + 3H+. When ferredoxin from Clostridium pasteurianum, NAD+, and the enzyme were incubated at pH 7.0 under 100% H2 in the gas phase (E0′ = −414 mV), more than 95% of the ferredoxin (E0′ = −400 mV) was reduced, which indicated that ferredoxin reduction with H2 is driven by the exergonic reduction of NAD+ (E0′ = −320 mV) with H2. In the absence of NAD+, ferredoxin was not reduced. We identified the genes encoding HydABC within the transcriptional unit hydCBAX and mapped the transcription start site." @default.
• W2034985989 created "2016-06-24" @default.
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• W2034985989 date "2013-01-11" @default.
• W2034985989 modified "2023-10-16" @default.
• W2034985989 title "A Reversible Electron-Bifurcating Ferredoxin- and NAD-Dependent [FeFe]-Hydrogenase (HydABC) in Moorella thermoacetica" @default.
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• W2034985989 doi "https://doi.org/10.1128/jb.02158-12" @default.
• W2034985989 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3591994" @default.
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