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Cited by 140Metalloenzymes and iron-sulfur proteinsAnaerobic Digestion and Biogas ProductionEnzyme Structure and Function

The DOI matches its Crossref record; 52 of the 55 references it cites were found in a registry or an index.

A Reversible Electron-Bifurcating Ferredoxin- and NAD-Dependent [FeFe]-Hydrogenase (HydABC) in Moorella thermoacetica

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Wang, S., Huang, H., Kahnt, J., Thauer, R. K.·2013·Journal of Bacteriology
DOI 10.1128/jb.02158-12PMC PMC3591994
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Abstract

Moorella thermoacetica was long the only model organism used to study the biochemistry of acetogenesis from CO(2). Depending on the growth substrate, this Gram-positive bacterium can either form H(2) or consume it. Despite the importance of H(2) 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 H(2) formation and H(2) uptake. The purified heterotrimeric iron-sulfur flavoprotein (HydABC) catalyzed the coupled reduction of ferredoxin (Fd) and NAD(+) with H(2) 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 H(2) with reduced ferredoxin and NADH, at a specific rate of about 10 μmol min(-1) mg protein(-1) in the stoichiometry Fd(ox) + NAD(+) + 2H(2) Fd(red)(2-) + NADH + 3H(+). When ferredoxin from Clostridium pasteurianum, NAD(+), and the enzyme were incubated at pH 7.0 under 100% H(2) in the gas phase (E(0)' = -414 mV), more than 95% of the ferredoxin (E(0)' = -400 mV) was reduced, which indicated that ferredoxin reduction with H(2) is driven by the exergonic reduction of NAD(+) (E(0)' = -320 mV) with H(2). 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.

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Metadata

Authors
Wang, S., Huang, H., Kahnt, J., & Thauer, R. K.
Affiliations
  • Shandong University (CN)
  • Max Planck Institute for Terrestrial Microbiology (DE)
ORCID
Venue
Journal of Bacteriology
Publisher
American Society for Microbiology
Published
2013-01-11
Volume
195
Issue
6
Pages
1267-1275
ISSN
0021-9193 (ISSN-L)
DOI
10.1128/jb.02158-12
PMC
PMC3591994
OpenAlex
W2034985989
Cited by
140
References
55
Citations by year
2026: 6 · 2025: 6 · 2024: 10 · 2023: 11 · 2022: 14 · 2021: 8 · 2020: 10 · 2019: 8 · 2018: 13 · 2017: 7 · 2016: 12 · 2015: 14 · 2014: 14 · 2013: 7
FWCI
5.70
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
Max-Planck-Gesellschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Anaerobic Digestion and Biogas Production
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
[FeFe]-hydrogenase, Moorella thermoacetica, electron bifurcation, hydrogenase, hydrogen production, hydrogen absorption, ferredoxin, NAD+ reduction, iron-sulfur flavoprotein, acetogenesis, transcription start sites
MeSH terms
Ferredoxins, Flavoproteins, Genes, Bacterial, Hydrogen, Hydrogenase, Iron-Sulfur Proteins, Molecular Sequence Data, NAD, Transcription Initiation Site, Biocatalysis, Moorella

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