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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q72EY4
• Protein Description: SubName: Full=Ech hydrogenase, subunit EchA, putative {ECO:0000313|EMBL:AAS94917.1};
• Gene Information: OrderedLocusNames=DVU_0434 {ECO:0000313|EMBL:AAS94917.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Not specified in UniProt
• Key Domains: CPA3_Na-H_Antiporter_A. (IPR050616); ND/Mrp_TM. (IPR001750); Proton_antipo_N. (IPR001516); Proton_antipo_M (PF00361); Proton_antipo_N (PF00662)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72EY4" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Q72EY4' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Q72EY4 (gene ID: Q72EY4, UniProt: Q72EY4) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q72EY4
• Protein Description: SubName: Full=Ech hydrogenase, subunit EchA, putative {ECO:0000313|EMBL:AAS94917.1};
• Gene Information: OrderedLocusNames=DVU_0434 {ECO:0000313|EMBL:AAS94917.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Not specified in UniProt
• Key Domains: CPA3_Na-H_Antiporter_A. (IPR050616); ND/Mrp_TM. (IPR001750); Proton_antipo_N. (IPR001516); Proton_antipo_M (PF00361); Proton_antipo_N (PF00662)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72EY4" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Q72EY4' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Q72EY4 (gene ID: Q72EY4, UniProt: Q72EY4) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan summary
- Verified identity. Q72EY4 corresponds to DVU_0434 from Desulfovibrio vulgaris Hildenborough, annotated as an energy‑converting [NiFe]-hydrogenase (Ech) membrane subunit EchA with MrpA-like antiporter domains, consistent with the antiporter-like membrane subunits that anchor Ech complexes. This aligns with Ech architecture reported for Desulfovibrio spp. and other anaerobes (schoelmerich2020energyconvertinghydrogenasesthe pages 1-2, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Literature availability. Direct primary literature tied specifically to DVU_0434 is limited; therefore, functional assignment is inferred from Ech complex biochemistry, the conserved multi-subunit architecture, and antiporter-like domains (MrpA-like) characteristic of EchA across taxa, plus recent experimental work in closely related bacterial systems (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2, baum2024theenergyconvertinghydrogenase pages 1-2, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).

Comprehensive research report: Q72EY4 (DVU_0434, EchA) in Desulfovibrio vulgaris Hildenborough

1) Key concepts and definitions
- Energy‑converting [NiFe]-hydrogenases (Ech). Ech are group 4 [NiFe]-hydrogenase complexes that couple H2/2H+ interconversion with transmembrane ion-gradient formation (Δμ̃ion) for energy conservation, typically linking low-potential ferredoxin (Fd) to proton reduction and H2 evolution (or the reverse) (Schoelmerich & Müller 2020, Cellular and Molecular Life Sciences, Oct 2020; https://doi.org/10.1007/s00018-019-03329-5) (schoelmerich2020energyconvertinghydrogenasesthe pages 1-2). Architecturally, a canonical Ech comprises six core subunits echABCDEF: two membrane-integral, antiporter-like subunits (EchA, EchB) and four hydrophilic electron‑transfer/catalytic subunits (EchC, EchD, EchE—the large hydrogenase subunit, and EchF) (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- EchA (MrpA-like antiporter-like subunit). EchA is one of the hydrophobic, membrane-embedded subunits thought to form the ion-translocating module of Ech; sequence and functional analogy relate EchA to MrpA/antiporter components and respiratory complex I subunits (schoelmerich2020energyconvertinghydrogenasesthe pages 16-17). DVU_0434 (Q72EY4) is annotated as EchA and contains antiporter-associated domains (CPA3/ND/Mrp_TM/Proton_antipo_N/M) consistent with this role (user-supplied UniProt context; inference aligned with general Ech architecture) (schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Directionality and partners. Ech catalyzes reversible reactions between Fdred and H+ ↔ H2 + Fdox, linking H2 metabolism to chemiosmotic energy conservation; electron partners include low‑potential carriers such as ferredoxin and sometimes modules handling CO or formate in larger operon contexts (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18).

2) Recent developments and latest research (priority 2023–2024)
- Bacterial Ech physiology and genetics (2024). In Thermoanaerobacter kivui, a thermophilic acetogen encoding two Ech clusters, an ech2 cluster deletion impaired growth on ferredoxin‑dependent substrates (pyruvate and CO) while sparing growth on sugars and H2+CO2, demonstrating Ech’s roles in redox balancing and energy conservation and functional differentiation among paralogs (Microbiology Spectrum, Apr 2024; https://doi.org/10.1128/spectrum.03380-23) (baum2024theenergyconvertinghydrogenase pages 1-2). These findings reinforce the model that Ech couples Fdred oxidation to H+ reduction for H2 evolution with concomitant chemiosmotic energy conservation and that membrane Ech subunits underpin energy-coupling in bacteria.
- Ion coupling evidence refined. Biochemical work summarized in the 2020 review collating data across organisms shows Fd-dependent H2 evolution-driven ATP synthesis in membrane vesicles is abolished by protonophores but not sodium ionophores (e.g., Methanosarcina/Methanococcus systems), supporting proton coupling; this remains a reference point for interpreting bacterial Ech ion coupling (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10). Together with 2024 bacterial genetics, this suggests bacterial Ech commonly employ H+ translocation, though the exact stoichiometry can vary and modular variants can interface with Na+ modules in some systems (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18).

3) Primary function, substrate specificity, and biochemical pathway context
- Reaction and specificity. The Ech catalytic core (EchE/EchC) is a [NiFe]-hydrogenase that catalyzes 2H+ + 2e− ↔ H2, with electrons transferred to/from low-potential ferredoxin via EchF/EchC and multiple Fe‑S clusters; ferredoxin is a principal physiological partner (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2). Purified preparations showed high specific activities for H2 evolution with Fdred (Vmax ~90 U/mg; apparent Km Fd ≈ 1–7.5 µM), in line with tight Fd coupling (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10).
- Ion coupling. Multiple lines of evidence indicate Ech establishes a proton motive force (Δp) during Fd-dependent H2 evolution or utilizes Δp during H2 oxidation for Fd reduction; ATP formation linked to Fd→H2 was sensitive to protonophores but insensitive to Na+ ionophores in inverted vesicles (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10). Broader group 4 complexes can be modular and, in some organisms, interface with Na+ antiporter modules; however, the core Ech system—and by analogy EchA—most often supports H+ translocation (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Pathways in Desulfovibrio context. Desulfovibrio spp. encode echABCDEF operons and couple H2 metabolism to energy conservation in sulfate‑reducing respiration, where Ech likely supports redox balancing between periplasmic H2 cycling and cytoplasmic low‑potential carriers for central enzymes (e.g., pyruvate:ferredoxin oxidoreductase, CODH/ACS) (inference based on conserved Ech roles and Desulfovibrio reports in the review) (schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2). While DVU_0434‑specific experiments were not recovered here, the architecture and biochemistry are strongly conserved and consistent with EchA as the ion‑translocating membrane component.

4) Localization, structure/architecture, and operon organization
- Localization. Ech is membrane-associated; EchA and EchB are hydrophobic membrane subunits that anchor the complex and mediate vectorial ion translocation across the cytoplasmic membrane (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Architecture. The minimal core is EchA/B (membrane antiporter-like), EchC (small [NiFe]-hydrogenase subunit with Fe‑S clusters), EchE (large [NiFe]-hydrogenase catalytic subunit), and electron‑transfer subunits EchD/EchF (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10). Ech belongs to group 4 [NiFe] hydrogenases and is evolutionarily related to respiratory complex I, consistent with the antiporter-like domain content of EchA (schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Operon context. Ech genes typically occur as echABCDEF clusters, sometimes paired or embedded in larger modules with formate dehydrogenase and antiporter loci in diverse anaerobes; Desulfovibrio species are reported to harbor ech clusters with differential expression across growth conditions, pointing to specialization for gradient formation versus ferredoxin pool balancing (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18).

5) Physiological role and phenotypes
- Energy conservation and redox balancing. Ech links ferredoxin pools to proton reduction and chemiosmotic energy conservation, supporting ATP synthesis via the proton motive force. In acetogens and methanogens, Ech is essential for growth on substrates requiring ferredoxin cycling (e.g., CO, pyruvate), and genetic loss causes substrate‑specific growth defects (2024 T. kivui Δech2) (baum2024theenergyconvertinghydrogenase pages 1-2). Earlier genetics/biochemistry in methanogens show Ech’s necessity for growth on H2/CO2 and acetate, integrating with ferredoxin‑linked central enzymes (major2006theroleof pages 21-25).
- Directionality in situ. Ech can operate bidirectionally: (i) Fdred → H2 + Δp during energy conservation, or (ii) H2 + Δp → Fdred to supply low‑potential electrons to Fd‑dependent enzymes under alternative conditions (schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2). This flexibility is consistent with Desulfovibrio physiology, where H2 can be both an electron donor and a metabolite exchanged with syntrophic partners.

6) Expert opinions and authoritative synthesis
- The 2020 Cell. Mol. Life Sci. review frames Ech as a modular, complex I‑related machine that commonly generates a proton motive force, with antiporter‑like membrane subunits (EchA/B) being responsible for ion translocation. It emphasizes Ech’s widespread occurrence in bacteria including Desulfovibrio and its centrality in linking H2 metabolism to bioenergetics (Oct 2020; https://doi.org/10.1007/s00018-019-03329-5) (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Foundational work summarized in the same review documents Fd↔H2 coupling and chemiosmotic energy conservation by Ech with proton coupling as the predominant mechanism, while recognizing modularity that may permit Na+ coupling in special contexts (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2).

7) Relevant statistics and data points
- Enzymology: Purified Ech preparations (e.g., Methanosarcina) exhibited Vmax ~90 U/mg for H2 evolution with Fdred and apparent Km for ferredoxin in the low micromolar range (~1–7.5 µM), highlighting tight Fd coupling (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10).
- Genetics/physiology: Deletion of ech2 in Thermoanaerobacter kivui impaired growth on ferredoxin-dependent substrates (pyruvate, CO), but not on sugars or H2+CO2, demonstrating role specificity within Ech paralogs for redox balancing and energy conservation (Microbiology Spectrum, Apr 2024; https://doi.org/10.1128/spectrum.03380-23) (baum2024theenergyconvertinghydrogenase pages 1-2).

8) Real‑world applications and implementations
- Bioenergy and gas fermentation. The 2024 T. kivui study highlights Ech’s relevance to bioindustrial gas fermentation at elevated temperatures by enabling efficient H2/CO2 utilization and ferredoxin‑linked electron flow; understanding Ech function and redundancy aids engineering for H2, acetate, or biofuel production (Apr 2024; https://doi.org/10.1128/spectrum.03380-23) (baum2024theenergyconvertinghydrogenase pages 1-2).
- Environmental anaerobes. Given Ech’s role in energy conservation in sulfate reducers and methanogens, the complex is pertinent to anaerobic digestion, syntrophic H2 transfer, and subsurface biogeochemistry; the established proton coupling mechanism informs strategies to manipulate redox balance and ATP yields in engineered systems (schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2).

9) Evidence synthesis for DVU_0434 (Q72EY4, EchA) in D. vulgaris Hildenborough
- Identity verification. DVU_0434 is the EchA subunit of an echABCDEF cluster in D. vulgaris Hildenborough per UniProt-like annotation provided. EchA is a MrpA-like membrane subunit expected to form part of the ion‑translocating module (schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Function inference. By homology and complex-level biochemistry, DVU_0434 participates in a membrane Ech that couples Fd/H2 interconversion to proton motive force generation. The most strongly supported coupling ion is H+, based on protonophore sensitivity and sodium ionophore insensitivity of ATP formation during Fd→H2 in model systems, and reinforced by recent bacterial genetics demonstrating chemiosmotic coupling in Ech‑type systems (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, baum2024theenergyconvertinghydrogenase pages 1-2, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Localization. DVU_0434 is membrane-integral, embedded in the cytoplasmic membrane as part of the Ech complex (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Pathway role in Desulfovibrio. In sulfate‑reducing metabolism, Ech likely (i) conserves energy when disposing of reduced ferredoxin as H2 and (ii) provides low‑potential electrons by reversing under appropriate conditions, integrating with central ferredoxin‑dependent enzymes; expression of ech clusters is known to vary with growth conditions across taxa and is reported to be differential in D. vulgaris according to the review synthesis (schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 1-2).

Limitations and data gaps
- Direct, DVU_0434‑specific experimental studies (e.g., gene deletion, biochemistry in D. vulgaris Hildenborough) were not recovered here; therefore, aspects of function and ion coupling for Q72EY4 are inferred from conserved architecture and experimental work in closely related systems. Future work should validate ion coupling stoichiometry and physiological roles for the D. vulgaris Ech complex in defined electron‑donor/acceptor regimes.

References (URLs and dates)
- Schoelmerich MC, Müller V. Energy-converting hydrogenases: the link between H2 metabolism and energy conservation. Cellular and Molecular Life Sciences. 77:1461–1481. Published Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5 (schoelmerich2020energyconvertinghydrogenasesthe pages 1-2, schoelmerich2020energyconvertinghydrogenasesthe pages 8-10, schoelmerich2020energyconvertinghydrogenasesthe pages 5-7, schoelmerich2020energyconvertinghydrogenasesthe pages 17-18, schoelmerich2020energyconvertinghydrogenasesthe pages 16-17).
- Baum C, Zeldes B, Poehlein A, Daniel R, Müller V, Basen M. The energy-converting hydrogenase Ech2 is important for the growth of the thermophilic acetogen Thermoanaerobacter kivui on ferredoxin-dependent substrates. Microbiology Spectrum. Published Apr 2024. URL: https://doi.org/10.1128/spectrum.03380-23 (baum2024theenergyconvertinghydrogenase pages 1-2).
- Major TA. The role of the energy-conserving hydrogenase B in autotrophy and the characterization of sulfur metabolism in Methanococcus maripaludis. 2006. (Foundational description of Ech/Ehb subunits and roles; citation lacks a stable URL in the retrieved excerpt) (major2006theroleof pages 74-82, major2006theroleof pages 21-25).

References

1. (schoelmerich2020energyconvertinghydrogenasesthe pages 1-2): Marie Charlotte Schoelmerich and Volker Müller. Energy-converting hydrogenases: the link between h2 metabolism and energy conservation. Cellular and Molecular Life Sciences, 77:1461-1481, Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5, doi:10.1007/s00018-019-03329-5. This article has 86 citations and is from a domain leading peer-reviewed journal.

2. (schoelmerich2020energyconvertinghydrogenasesthe pages 16-17): Marie Charlotte Schoelmerich and Volker Müller. Energy-converting hydrogenases: the link between h2 metabolism and energy conservation. Cellular and Molecular Life Sciences, 77:1461-1481, Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5, doi:10.1007/s00018-019-03329-5. This article has 86 citations and is from a domain leading peer-reviewed journal.

3. (schoelmerich2020energyconvertinghydrogenasesthe pages 8-10): Marie Charlotte Schoelmerich and Volker Müller. Energy-converting hydrogenases: the link between h2 metabolism and energy conservation. Cellular and Molecular Life Sciences, 77:1461-1481, Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5, doi:10.1007/s00018-019-03329-5. This article has 86 citations and is from a domain leading peer-reviewed journal.

4. (baum2024theenergyconvertinghydrogenase pages 1-2): Christoph Baum, Benjamin Zeldes, Anja Poehlein, Rolf Daniel, Volker Müller, and Mirko Basen. The energy-converting hydrogenase ech2 is important for the growth of the thermophilic acetogen thermoanaerobacter kivui on ferredoxin-dependent substrates. Microbiology Spectrum, Apr 2024. URL: https://doi.org/10.1128/spectrum.03380-23, doi:10.1128/spectrum.03380-23. This article has 10 citations and is from a domain leading peer-reviewed journal.

5. (schoelmerich2020energyconvertinghydrogenasesthe pages 5-7): Marie Charlotte Schoelmerich and Volker Müller. Energy-converting hydrogenases: the link between h2 metabolism and energy conservation. Cellular and Molecular Life Sciences, 77:1461-1481, Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5, doi:10.1007/s00018-019-03329-5. This article has 86 citations and is from a domain leading peer-reviewed journal.

6. (schoelmerich2020energyconvertinghydrogenasesthe pages 17-18): Marie Charlotte Schoelmerich and Volker Müller. Energy-converting hydrogenases: the link between h2 metabolism and energy conservation. Cellular and Molecular Life Sciences, 77:1461-1481, Oct 2020. URL: https://doi.org/10.1007/s00018-019-03329-5, doi:10.1007/s00018-019-03329-5. This article has 86 citations and is from a domain leading peer-reviewed journal.

7. (major2006theroleof pages 21-25): TA Major. The role of the energy conserving hydrogenase b in autotrophy and the characterization of sulfur metabolism in methanococcus maripaludis. Unknown journal, 2006.

8. (major2006theroleof pages 74-82): TA Major. The role of the energy conserving hydrogenase b in autotrophy and the characterization of sulfur metabolism in methanococcus maripaludis. Unknown journal, 2006.

Citations

1. schoelmerich2020energyconvertinghydrogenasesthe pages 1-2
2. schoelmerich2020energyconvertinghydrogenasesthe pages 16-17
3. baum2024theenergyconvertinghydrogenase pages 1-2
4. schoelmerich2020energyconvertinghydrogenasesthe pages 8-10
5. major2006theroleof pages 21-25
6. schoelmerich2020energyconvertinghydrogenasesthe pages 5-7
7. schoelmerich2020energyconvertinghydrogenasesthe pages 17-18
8. major2006theroleof pages 74-82
9. NiFe
10. https://doi.org/10.1007/s00018-019-03329-5
11. https://doi.org/10.1128/spectrum.03380-23
12. https://doi.org/10.1007/s00018-019-03329-5,
13. https://doi.org/10.1128/spectrum.03380-23,