Cited by 447Metalloenzymes and iron-sulfur proteinsAnaerobic Digestion and Biogas ProductionEnzyme Structure and Function

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The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production

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Schut, Gerrit J., Adams, Michael W. W.·2009·Journal of Bacteriology

DOI 10.1128/jb.01582-08PMC PMC2698477

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Abstract

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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Authors: Schut, G. J., & Adams, M. W. W.
Affiliations: University of Georgia (US)
ORCID: Schut, Gerrit J.
Adams, Michael W. W.
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
DOI: 10.1128/jb.01582-08
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Science Foundation
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: 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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The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production

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