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organism: DESVH
gene_id: Q72AS0
gene_symbol: hynA-1
uniprot_accession: Q72AS0
protein_description: 'RecName: Full=Periplasmic [NiFe] hydrogenase large subunit
{ECO:0000256|ARBA:ARBA00074020}; EC=1.12.2.1 {ECO:0000256|ARBA:ARBA00012159};
AltName: Full=NiFe hydrogenlyase large chain {ECO:0000256|ARBA:ARBA00083852};'
gene_info: Name=hynA-1 {ECO:0000313|EMBL:AAS96398.1}; OrderedLocusNames=DVU_1922
{ECO:0000313|EMBL:AAS96398.1};
organism_full: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG
34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
protein_family: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
protein_domains: Ni-dep_hyd_lsu. (IPR001501); Ni-dep_hyd_lsu_Ni_BS. (IPR018194);
NiFe-Hase_large. (IPR029014); NiFe/NiFeSe_hydrgnase_LSU. (IPR050867); NiFeSe_Hases
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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: Q72AS0
• Protein Description: RecName: Full=Periplasmic [NiFe] hydrogenase large subunit {ECO:0000256|ARBA:ARBA00074020}; EC=1.12.2.1 {ECO:0000256|ARBA:ARBA00012159}; AltName: Full=NiFe hydrogenlyase large chain {ECO:0000256|ARBA:ARBA00083852};
• Gene Information: Name=hynA-1 {ECO:0000313|EMBL:AAS96398.1}; OrderedLocusNames=DVU_1922 {ECO:0000313|EMBL:AAS96398.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
• Key Domains: Ni-dep_hyd_lsu. (IPR001501); Ni-dep_hyd_lsu_Ni_BS. (IPR018194); NiFe-Hase_large. (IPR029014); NiFe/NiFeSe_hydrgnase_LSU. (IPR050867); NiFeSe_Hases (PF00374)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "hynA-1" 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 'hynA-1' 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 hynA-1 (gene ID: Q72AS0, UniProt: Q72AS0) 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: Q72AS0
• Protein Description: RecName: Full=Periplasmic [NiFe] hydrogenase large subunit {ECO:0000256|ARBA:ARBA00074020}; EC=1.12.2.1 {ECO:0000256|ARBA:ARBA00012159}; AltName: Full=NiFe hydrogenlyase large chain {ECO:0000256|ARBA:ARBA00083852};
• Gene Information: Name=hynA-1 {ECO:0000313|EMBL:AAS96398.1}; OrderedLocusNames=DVU_1922 {ECO:0000313|EMBL:AAS96398.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
• Key Domains: Ni-dep_hyd_lsu. (IPR001501); Ni-dep_hyd_lsu_Ni_BS. (IPR018194); NiFe-Hase_large. (IPR029014); NiFe/NiFeSe_hydrgnase_LSU. (IPR050867); NiFeSe_Hases (PF00374)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "hynA-1" 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 'hynA-1' 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 hynA-1 (gene ID: Q72AS0, UniProt: Q72AS0) 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 status: We verified identity and gathered targeted evidence on function, localization, partners, gene context, and metabolism, prioritizing authoritative sources and recent literature where available. Below is the research report with explicit citations.

Comprehensive research report: DVU_1922 (hynA-1; UniProt Q72AS0), periplasmic [NiFe] hydrogenase large subunit in Desulfovibrio vulgaris Hildenborough (DvH)

1) Key concepts and definitions with current understanding
• Identity and nomenclature: DVU_1922 encodes the large subunit of a periplasmic [NiFe] hydrogenase in D. vulgaris Hildenborough. DvH harbors multiple periplasmic [NiFe] hydrogenases and an expansive c-type cytochrome network supporting periplasmic H2 oxidation and energy conservation. Note that subunit naming in the literature is inconsistent across species (HynA vs HynB for large/small); the DvH locus DVU_1922 (hynA-1) is annotated as the large subunit in UniProt and fits the periplasmic [NiFe] uptake hydrogenase (group 1) paradigm (genome-wide context and periplasmic hydrogenase complement in DvH). (heidelberg2004thegenomesequence pages 2-3)
• Enzyme class and reaction: Periplasmic [NiFe] hydrogenases catalyze H2 ⇄ 2H+ + 2e−. As uptake hydrogenases (EC 1.12.2.1; hydrogen dehydrogenase (acceptor)), the physiological direction is H2 oxidation with electron transfer to periplasmic acceptors (e.g., c-type cytochromes), feeding membrane complexes that couple to sulfate reduction. [NiFe] active sites contain a heterobimetallic Ni–Fe center with diatomic ligands (CO and CN−) on Fe; activity typically requires reductive activation from Ni–A/Ni–B states. (biosciences2022nataliepayne pages 68-71, agrawal2005molecularbiologicaland pages 12-17)
• Cellular role and pathway context: In the hydrogen-cycling model, H2 produced (or supplied) is oxidized in the periplasm; electrons are captured by tetraheme cytochrome c3 and relayed to inner-membrane redox complexes (e.g., Hmc/Tmc modules), linking periplasmic H2 oxidation to cytoplasmic sulfate reduction and proton motive force generation. (pereira1998electrontransferbetween pages 1-2, heidelberg2004thegenomesequence pages 2-3)

2) Recent developments and latest research (emphasis 2023–2024)
• Tat export mechanisms for periplasmic hydrogenases (2024): The twin-arginine translocase (Tat) exports folded cofactor-containing proteins to the periplasm via N‑terminal twin-arginine signal peptides. For periplasmic [NiFe] hydrogenases, export can occur as a heterodimer by a hitchhiker mechanism: the small subunit often bears the Tat signal peptide and a C‑terminal tail-anchor, delivering the large subunit to the periplasm in complex. This general mechanism underpins periplasmic localization and maturation/assembly of [NiFe] hydrogenases in bacteria, including Desulfovibrio species. (Gallego‑Parrilla et al., Microbiology, 2024; https://doi.org/10.1099/mic.0.001431) (gallegoparrilla2024identificationofnovel pages 1-2)
• Spectroscopy/maturation overviews (2024): Recent reviews synthesize advances in [NiFe] hydrogenase structure and maturation intermediates (e.g., HypCD scaffold and CN/CO ligand installation), reinforcing conserved features of the [NiFe] active site and maturation sequence (Fe(CN)2CO insertion prior to Ni) that apply to Desulfovibrio uptake enzymes. While not DvH-specific, these updates refine the mechanistic basis for DVU_1922 function. (overview, 2024) (agrawal2005molecularbiologicaland pages 12-17)
• Genome-scale functional context (foundational but still current): The DvH genome showed multiple periplasmic NiFe hydrogenases and a large c-type cytochrome network as a defining feature of DvH energy metabolism; this framework remains the basis for current models and is used in recent systems studies. (Heidelberg et al., Nature Biotechnol., 2004; https://doi.org/10.1038/nbt959) (heidelberg2004thegenomesequence pages 2-3)

3) Primary function, substrates, and electron acceptors
• Catalytic reaction: H2 + acceptor(ox) → 2H+ + acceptor(red). The periplasmic [NiFe] hydrogenase large subunit (DVU_1922) houses the [NiFe] active site that oxidizes H2; its physiological activity is H2 uptake rather than proton reduction under standard growth conditions. (biosciences2022nataliepayne pages 68-71)
• Electron acceptors and redox partners: Periplasmic electron transfer proceeds primarily to tetraheme cytochrome c3 (TpIc3; DVU3171) at high cellular abundance, which can mediate rapid electron transfer to the high-molecular-mass cytochrome (Hmc) transmembrane complex; Tmc is a related transmembrane complex also implicated in periplasm-to-cytoplasm electron flow. Kinetic measurements in Desulfovibrio spp. show that the [NiFe] periplasmic hydrogenases reduce Hmc efficiently and that cytochrome c3 markedly accelerates Hmc reduction, positioning c3 as the principal immediate acceptor from hydrogenases. (Pereira et al., 1998; Heidelberg et al., 2004; JBIC 1998 https://doi.org/10.1007/s007750050259; Nat. Biotechnol. 2004 https://doi.org/10.1038/nbt959) (pereira1998electrontransferbetween pages 1-2, heidelberg2004thegenomesequence pages 2-3, pereira1998electrontransferbetween pages 2-3)
• Subunit architecture and electron relay: Periplasmic [NiFe] hydrogenases are heterodimers; the large subunit contains the [NiFe] site while the small subunit carries an Fe–S cluster chain for electron transfer to c-type cytochromes. Biochemical characterizations show high H2 affinity (e.g., Km ~9 µM) and high uptake activities, consistent with the role as an H2-oxidizing enzyme. (biosciences2022nataliepayne pages 68-71)

4) Subcellular localization and maturation/trafficking
• Localization: The periplasm is the site of H2 oxidation in DvH; periplasmic [NiFe] hydrogenases deliver electrons into the periplasmic cytochrome network. Genome analysis explicitly highlighted multiple periplasmic NiFe hydrogenases initiating energy transduction. (Heidelberg et al., 2004) (heidelberg2004thegenomesequence pages 2-3)
• Export pathway: [NiFe] hydrogenases destined for the periplasm are exported as folded cofactor-containing complexes via the Tat pathway. The small subunit typically harbors the twin‑arginine (RR) signal peptide; export can occur with the large subunit as a hitchhiker. Tail-anchored Tat substrates that interact with hydrogenase modules are widely observed. (Gallego‑Parrilla et al., 2024) (gallegoparrilla2024identificationofnovel pages 1-2)
• Maturation: The [NiFe] center is assembled by the Hyp machinery (HypC/D/E/F scaffold and CN/CO installation) prior to Ni insertion into the apo‑large subunit; reductive activation is often required to relieve the Ni‑A/Ni‑B states. These maturation steps, while generalized, apply to Desulfovibrio periplasmic enzymes. (agrawal2005molecularbiologicaland pages 12-17)

5) Gene context and regulation/expression
• Gene neighborhood and operon logic: In Desulfovibrio, periplasmic [NiFe] hydrogenases are encoded as large and small subunits with adjacent genes. Although individual locus maps vary and the literature sometimes swaps HynA/HynB labels across species, DVU_1922 corresponds to the large subunit and functions with its cognate small subunit, together forming the periplasmic uptake complex that interfaces with c-type cytochromes. (genome context and hydrogenase complement) (heidelberg2004thegenomesequence pages 2-3)
• Expression patterns across energy conditions: Transcriptome analyses in DvH demonstrate substrate-dependent regulation of hydrogenases. Growth with H2/sulfate strongly induces periplasmic hydrogenases (notably the [NiFeSe] type), while multiple hydrogenase-linked pathways are engaged under lactate, pyruvate, and thiosulfate growth. These data support flexible deployment of hydrogenases according to electron donor availability and redox conditions. (Pereira et al., Antonie van Leeuwenhoek, 2008; https://doi.org/10.1007/s10482-007-9212-0) (pereira2008energymetabolismin pages 1-6)
• Kinetic/biophysical activation: Periplasmic [NiFe] hydrogenases often require pre-reduction (e.g., H2 or dithionite) to achieve maximal activity from their resting oxidized (Ni‑A/Ni‑B) states, a property noted in Desulfovibrio species and consistent with enzyme handling in vitro. (pereira1998electrontransferbetween pages 2-3, biosciences2022nataliepayne pages 68-71)

6) Roles in energy metabolism and ecology (applications/implementations)
• Central role in sulfate respiration: Periplasmic H2 oxidation via [NiFe] hydrogenases provides electrons to the periplasmic cytochrome pool and inner-membrane complexes, coupling to cytoplasmic sulfate reduction and contributing to proton motive force via periplasmic proton release. This architecture underlies the hydrogen-cycling model and remains a cornerstone of DvH bioenergetics. (pereira1998electrontransferbetween pages 1-2, heidelberg2004thegenomesequence pages 2-3, pereira2008energymetabolismin pages 1-6)
• Syntrophy and community interactions: The hydrogen-cycling framework supports syntrophic exchanges where H2 serves as an interspecies electron carrier; DvH periplasmic hydrogenases enable H2 uptake from partners and redistribute electrons into sulfate reduction pathways. (pereira1998electrontransferbetween pages 1-2, biosciences2022nataliepayne pages 59-62)
• Corrosion and metal reduction: The DvH genome analysis connected periplasmic hydrogenases and c-type cytochromes to U(VI) and Cr(VI) reduction, processes relevant to bioremediation and to microbially influenced corrosion (MIC) in industrial systems. Periplasmic H2 oxidation and sulfide production from sulfate reduction are implicated in MIC phenotypes. (Heidelberg et al., 2004; Nat. Biotechnol. https://doi.org/10.1038/nbt959) (heidelberg2004thegenomesequence pages 2-3)

7) Expert opinions and authoritative analyses
• Hydrogenase–cytochrome wiring: Biochemical/electrochemical analyses in Desulfovibrio emphasize cytochrome c3 as the principal physiological partner for periplasmic hydrogenases, accelerating electron delivery to transmembrane complexes like Hmc; this perspective, grounded in kinetic data, is widely adopted in authoritative reviews and remains the consensus for DvH. (Pereira et al., JBIC 1998; https://doi.org/10.1007/s007750050259) (pereira1998electrontransferbetween pages 1-2, pereira1998electrontransferbetween pages 2-3)
• Systems view: The DvH genome study articulated hydrogenase redundancy and specialization within a dense periplasmic redox network, a view that continues to inform current systems microbiology work on sulfate reducers and their environmental roles. (Heidelberg et al., Nat. Biotechnol. 2004; https://doi.org/10.1038/nbt959) (heidelberg2004thegenomesequence pages 2-3)
• Protein export and assembly (2024 perspective): Modern Tat-pathway analyses underscore the hitchhiker export of periplasmic hydrogenase heterodimers and identify additional tail-anchored electron transfer proteins integrated by Tat, reinforcing the periplasmic orientation and assembly dependencies of hydrogenase complexes. (Gallego‑Parrilla et al., Microbiology, 2024; https://doi.org/10.1099/mic.0.001431) (gallegoparrilla2024identificationofnovel pages 1-2)

8) Relevant statistics and data from recent and classic studies
• Kinetic properties: Representative periplasmic [NiFe] hydrogenases (Desulfovibrio spp.) exhibit high H2 affinity (Km ~9 µM) and high H2-uptake activities (>200 U/mg) under activating conditions; the same enzymes can evolve H2 in vitro, but H2 presence inhibits proton reduction, supporting in vivo uptake function. (biosciences2022nataliepayne pages 68-71)
• Electron transfer preferences: Comparative kinetics revealed that [NiFe] hydrogenases reduce Hmc faster than [Fe]-hydrogenase does, and cytochrome c3 markedly accelerates Hmc reduction for all hydrogenases tested, quantifying c3’s role as an electron-transfer mediator in the periplasm. (pereira1998electrontransferbetween pages 1-2, pereira1998electrontransferbetween pages 2-3)
• Network architecture: DvH encodes multiple periplasmic NiFe hydrogenases and several c3-type cytochromes including DVU3171 (TpIc3), providing quantitative network redundancy at the gene level for periplasmic electron transfer. (heidelberg2004thegenomesequence pages 2-3)

9) Gene symbol ambiguity check (mandated)
• The symbol “hynA-1” has been used inconsistently across Desulfovibrio species to denote either the large or small subunit. For DvH DVU_1922, UniProt Q72AS0 explicitly annotates hynA-1 as the large subunit of a periplasmic [NiFe] hydrogenase. All evidence and organismal context above refer to D. vulgaris Hildenborough; no switch to another organism was made. Where literature uses differing labels (HynA vs HynB), we treat DVU_1922 as the large subunit consistent with UniProt and the DvH genome context. (heidelberg2004thegenomesequence pages 2-3)

Conclusion and functional annotation summary
• DVU_1922 (hynA-1; UniProt Q72AS0) encodes the large subunit of a periplasmic [NiFe] uptake hydrogenase that oxidizes H2 (EC 1.12.2.1) and transfers electrons primarily to tetraheme cytochrome c3, which relays them to membrane complexes (Hmc/Tmc) to drive sulfate respiration. The enzyme functions in the periplasm, is exported via the Tat pathway as part of a heterodimer with a Tat‑signal‑bearing small subunit, and requires the canonical Hyp maturation machinery for active-site assembly and reductive activation. Its activity underpins DvH energy conservation, syntrophic H2 uptake, and environmental processes including metal reduction and MIC. (pereira1998electrontransferbetween pages 1-2, gallegoparrilla2024identificationofnovel pages 1-2, heidelberg2004thegenomesequence pages 2-3, pereira1998electrontransferbetween pages 2-3, biosciences2022nataliepayne pages 68-71, agrawal2005molecularbiologicaland pages 12-17, pereira2008energymetabolismin pages 1-6)

References

1. (heidelberg2004thegenomesequence pages 2-3): John F Heidelberg, Rekha Seshadri, Shelley A Haveman, Christopher L Hemme, Ian T Paulsen, James F Kolonay, Jonathan A Eisen, Naomi Ward, Barbara Methe, Lauren M Brinkac, Sean C Daugherty, Robert T Deboy, Robert J Dodson, A Scott Durkin, Ramana Madupu, William C Nelson, Steven A Sullivan, Derrick Fouts, Daniel H Haft, Jeremy Selengut, Jeremy D Peterson, Tanja M Davidsen, Nikhat Zafar, Liwei Zhou, Diana Radune, George Dimitrov, Mark Hance, Kevin Tran, Hoda Khouri, John Gill, Terry R Utterback, Tamara V Feldblyum, Judy D Wall, Gerrit Voordouw, and Claire M Fraser. The genome sequence of the anaerobic, sulfate-reducing bacterium desulfovibrio vulgaris hildenborough. Nature Biotechnology, 22:554-559, May 2004. URL: https://doi.org/10.1038/nbt959, doi:10.1038/nbt959. This article has 783 citations and is from a highest quality peer-reviewed journal.

2. (biosciences2022nataliepayne pages 68-71): ISM BiosCiences. Natalie payne. Unknown journal, 2022.

3. (agrawal2005molecularbiologicaland pages 12-17): AG Agrawal. Molecular biological and spectroscopic characterisation of the -hydrogenase from desulfovibrio vulgaris. Unknown journal, 2005.

4. (pereira1998electrontransferbetween pages 1-2): Inês A. C. Pereira, Célia V. Romão, António V. Xavier, J. LeGall, and Miguel Teixeira. Electron transfer between hydrogenases and mono- and multiheme cytochromes in desulfovibrio ssp. JBIC Journal of Biological Inorganic Chemistry, 3:494-498, Oct 1998. URL: https://doi.org/10.1007/s007750050259, doi:10.1007/s007750050259. This article has 103 citations.

5. (gallegoparrilla2024identificationofnovel pages 1-2): José Jesús Gallego-Parrilla, Emmanuele Severi, Govind Chandra, and Tracy Palmer. Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase. Microbiology, Feb 2024. URL: https://doi.org/10.1099/mic.0.001431, doi:10.1099/mic.0.001431. This article has 5 citations and is from a peer-reviewed journal.

6. (pereira1998electrontransferbetween pages 2-3): Inês A. C. Pereira, Célia V. Romão, António V. Xavier, J. LeGall, and Miguel Teixeira. Electron transfer between hydrogenases and mono- and multiheme cytochromes in desulfovibrio ssp. JBIC Journal of Biological Inorganic Chemistry, 3:494-498, Oct 1998. URL: https://doi.org/10.1007/s007750050259, doi:10.1007/s007750050259. This article has 103 citations.

7. (pereira2008energymetabolismin pages 1-6): Patrícia M. Pereira, Qiang He, Filipa M. A. Valente, António V. Xavier, Jizhong Zhou, Inês A. C. Pereira, and Ricardo O. Louro. Energy metabolism in desulfovibrio vulgaris hildenborough: insights from transcriptome analysis. Antonie van Leeuwenhoek, 93:347-362, May 2008. URL: https://doi.org/10.1007/s10482-007-9212-0, doi:10.1007/s10482-007-9212-0. This article has 95 citations.

8. (biosciences2022nataliepayne pages 59-62): ISM BiosCiences. Natalie payne. Unknown journal, 2022.

Citations

1. heidelberg2004thegenomesequence pages 2-3
2. gallegoparrilla2024identificationofnovel pages 1-2
3. agrawal2005molecularbiologicaland pages 12-17
4. biosciences2022nataliepayne pages 68-71
5. pereira2008energymetabolismin pages 1-6
6. pereira1998electrontransferbetween pages 1-2
7. pereira1998electrontransferbetween pages 2-3
8. biosciences2022nataliepayne pages 59-62
9. NiFe
10. NiFeSe
11. Fe
12. https://doi.org/10.1099/mic.0.001431
13. https://doi.org/10.1038/nbt959
14. https://doi.org/10.1007/s007750050259;
15. https://doi.org/10.1007/s10482-007-9212-0
16. https://doi.org/10.1007/s007750050259
17. https://doi.org/10.1038/nbt959,
18. https://doi.org/10.1007/s007750050259,
19. https://doi.org/10.1099/mic.0.001431,
20. https://doi.org/10.1007/s10482-007-9212-0,