The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production
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The hyperthermophilic and anaerobic bacterium Thermotoga maritima ferments a wide variety of carbohydrates, producing acetate, CO 2 , and H 2 . Glucose is degraded through a classical Embden-Meyerhof pathway, and both NADH and reduced ferredoxin are generated. The oxidation of these electron carriers must be coupled to H 2 production, but the mechanism by which this occurs is unknown. The trimeric [FeFe]-type hydrogenase that was previously purified from T. maritima does not use either reduced ferredoxin or NADH as a sole electron donor. This problem has now been resolved by the demonstration that this hydrogenase requires the presence of both electron carriers for catalysis of H 2 production. The enzyme oxidizes NADH and ferredoxin simultaneously in an approximately 1:1 ratio and in a synergistic fashion to produce H 2 . It is proposed that the enzyme represents a new class of bifurcating [FeFe] hydrogenase in which the exergonic oxidation of ferredoxin (midpoint potential, −453 mV) is used to drive the unfavorable oxidation of NADH ( E 0 ′ = −320 mV) to produce H 2 ( E 0 ′ = −420 mV). From genome sequence analysis, it is now clear that there are two major types of [FeFe] hydrogenases: the trimeric bifurcating enzyme and the more well-studied monomeric ferredoxin-dependent [FeFe] hydrogenase. Almost one-third of the known H 2 -producing anaerobes appear to contain homologs of the trimeric bifurcating enzyme, although many of them also harbor one or more homologs of the simpler ferredoxin-dependent hydrogenase. The discovery of the bifurcating hydrogenase gives a new perspective on our understanding of the bioenergetics and mechanism of H 2 production and of anaerobic metabolism in general.
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Soluble confurcation processes have already been described, such as those involving multimeric hydrogenases and the NfnAB transhydrogenase.
“Soluble confurcation processes have already been described, such as those involving multimeric hydrogenases (NADH and Fdred as electron donors for H2 production) [196] and the NfnAB transhydrogenase (NADH and Fdred as electron donors for NADP+ reduction) [89,198].”
From Early bioenergetic evolution (2013) · cites this paper as [196]
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- Authors
- Schut, G. J., & Adams, M. W. W.
- Affiliations
- University of Georgia (US)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2009-07
- Volume
- 191
- Issue
- 13
- Pages
- 4451-4457
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC2698477
- OpenAlex
- W2043953512
- Cited by
- 447
- References
- 35
- Citations by year
- 2026: 13 · 2025: 15 · 2024: 13 · 2023: 23 · 2022: 27 · 2021: 28 · 2020: 31 · 2019: 36 · 2018: 30 · 2017: 27 · 2016: 31 · 2015: 26 · 2014: 32 · 2013: 34 · 2012: 33
- FWCI
- 12.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Engineering › Building and Construction › Anaerobic Digestion and Biogas Production
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Thermotoga maritima, anaerobic hydrogen production, ferredoxin, NADH, hyperthermophilic bacteria, carbohydrate fermentation, glucose metabolism, glycolysis, bioenergetics, hydrogenase mechanism
- MeSH terms
- Anaerobiosis, Bacterial Proteins, Ferredoxins, Hydrogen, Hydrogenase, Iron-Sulfur Proteins, Models, Biological, NAD, Genome, Bacterial, Thermotoga maritima
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