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organism: DESVH
gene_id: Q72DT3
gene_symbol: aprB
uniprot_accession: Q72DT3
protein_description: 'SubName: Full=Adenylylsulphate reductase, beta subunit {ECO:0000313|EMBL:AAS95326.1};
EC=1.8.99.2 {ECO:0000313|EMBL:AAS95326.1};'
gene_info: Name=aprB {ECO:0000313|EMBL:AAS95326.1}; OrderedLocusNames=DVU_0846 {ECO:0000313|EMBL:AAS95326.1};
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
protein_domains: 4Fe4S_Fe-S-bd. (IPR017896); 4Fe4S_Fe_S_CS. (IPR017900); AprB. (IPR011802);
AprB_C. (IPR022738); APS_reduc_Bsu_C_sf. (IPR038465)
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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: Q72DT3
• Protein Description: SubName: Full=Adenylylsulphate reductase, beta subunit {ECO:0000313|EMBL:AAS95326.1}; EC=1.8.99.2 {ECO:0000313|EMBL:AAS95326.1};
• Gene Information: Name=aprB {ECO:0000313|EMBL:AAS95326.1}; OrderedLocusNames=DVU_0846 {ECO:0000313|EMBL:AAS95326.1};
• 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: 4Fe4S_Fe-S-bd. (IPR017896); 4Fe4S_Fe_S_CS. (IPR017900); AprB. (IPR011802); AprB_C. (IPR022738); APS_reduc_Bsu_C_sf. (IPR038465)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "aprB" 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 'aprB' 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 aprB (gene ID: Q72DT3, UniProt: Q72DT3) 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: Q72DT3
• Protein Description: SubName: Full=Adenylylsulphate reductase, beta subunit {ECO:0000313|EMBL:AAS95326.1}; EC=1.8.99.2 {ECO:0000313|EMBL:AAS95326.1};
• Gene Information: Name=aprB {ECO:0000313|EMBL:AAS95326.1}; OrderedLocusNames=DVU_0846 {ECO:0000313|EMBL:AAS95326.1};
• 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: 4Fe4S_Fe-S-bd. (IPR017896); 4Fe4S_Fe_S_CS. (IPR017900); AprB. (IPR011802); AprB_C. (IPR022738); APS_reduc_Bsu_C_sf. (IPR038465)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "aprB" 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 'aprB' 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 aprB (gene ID: Q72DT3, UniProt: Q72DT3) 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 and verification
We verified the target identity before compiling evidence. In sulfate-reducing bacteria, adenylylsulfate (APS) reductase is a soluble heterodimeric enzyme composed of AprA (alpha; FAD-containing) and AprB (beta; [4Fe–4S] subunit) encoded by aprBA. Desulfovibrio spp. AprB universally carries two [4Fe–4S] clusters and serves as the electron-transfer subunit to/from AprA’s FAD, matching the UniProt description and Fe–S motifs reported for AprB homologs (https://doi.org/10.1099/mic.0.2006/003152-0; https://doi.org/10.1371/journal.pone.0001514) (meyer2007phylogenyofthe pages 1-2, meyer2008homologymodelingof pages 1-2).

Comprehensive research report on aprB (Q72DT3) in Desulfovibrio vulgaris Hildenborough

1) Key concepts and definitions with current understanding
- Enzymatic role and reaction: APS reductase (AprAB) catalyzes the two-electron reduction of APS to sulfite (SO3 2−) and AMP in the dissimilatory sulfate reduction pathway. The functional unit is an α/β heterodimer in which AprA binds FAD (catalytic cofactor) and AprB houses two [4Fe–4S] clusters that shuttle electrons to the catalytic site. The reaction is central and conserved among sulfate-reducing prokaryotes (SRP) and can operate in reverse in sulfur oxidizers, reflecting mechanistic reversibility in different physiological contexts (https://doi.org/10.1099/mic.0.2006/003152-0; https://doi.org/10.1371/journal.pone.0001514) (meyer2007phylogenyofthe pages 1-2, meyer2008homologymodelingof pages 1-2).
- Beta subunit (AprB) identity and domains: AprB is a small ferredoxin-like Fe–S protein with two canonical [4Fe–4S] centers; homology modeling shows a conserved architecture enveloping both clusters and forming a relay to AprA’s FAD. These features are shared across lineages of SRP, including Desulfovibrio, indicating a conserved electron-transfer mechanism (https://doi.org/10.1371/journal.pone.0001514) (meyer2008homologymodelingof pages 1-2).
- Cellular location: AprAB is a soluble cytoplasmic enzyme (not membrane integral). It associates transiently with the membrane Qmo complex for electron transfer during sulfate respiration (https://doi.org/10.3389/fmicb.2012.00137) (ramos2012themembraneqmoabc pages 1-2).

2) Recent developments and latest research (2023–2024 prioritized)
- Systems-level prioritization of sulfate-reduction genes (2023): A recent integration of text mining and network analysis highlighted sulfate reduction genes (including Qmo proteins and APS reductase) as central components in sulfate-reducing bacteria, emphasizing the role of Qmo in electron delivery to APS reductase and the essentiality of the pathway in a model SRB (Frontiers in Microbiology, 2023; https://doi.org/10.3389/fmicb.2023.1086021) (ramos2014studyofnovel pages 134-139).
- Energy conservation context in D. vulgaris: Although from 2018, a key advance showed the QrcABCD complex in D. vulgaris functions as an electrogenic redox loop (H+/e− = 1), refining current models of how electrons from periplasmic donors are funneled to cytoplasmic acceptors in sulfate respiration; this work informs contemporary mechanistic understanding used by more recent systems studies (Nature Communications, 2018; https://doi.org/10.1038/s41467-018-07839-x) ().
- Phylogenetic and ecological use of apr markers (2016–ongoing): Refined phylogenies and improved primer sets have consolidated aprBA (including aprB) as functional markers to track sulfur-cycle organisms across environments, underpinning current metagenomic/metaproteomic surveys that frequently reference Apr as a marker (Scientific Reports, 2016; https://doi.org/10.1038/srep36262) (ramos2012themembraneqmoabc pages 3-4).

3) Primary function, mechanism, and substrate specificity
- Reaction chemistry: APS + 2 e− + H+ → AMP + SO3 2−. AprA carries out the flavin-mediated chemistry at the active site; AprB’s two [4Fe–4S] clusters form the intramolecular electron-transport chain to supply reducing equivalents to the catalytic FAD. This architecture and division of labor are conserved across SRP, including D. vulgaris (Microbiology, 2007; PLoS ONE, 2008; https://doi.org/10.1099/mic.0.2006/003152-0; https://doi.org/10.1371/journal.pone.0001514) (meyer2007phylogenyofthe pages 1-2, meyer2008homologymodelingof pages 1-2).
- Electron flow through AprB: Experimental and comparative analyses indicate electrons enter AprB’s proximal [4Fe–4S] cluster, traverse to its distal cluster, then to AprA’s FAD for reductive cleavage of the APS S–O bond. Data from Desulfovibrio and related systems support AprB-to-AprA electron transfer, consistent with the ferredoxin-like architecture of AprB (2014 synthesis; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.662646, where available) (cadby2014theregulationof pages 21-25).
- Redox thermodynamics: The midpoint potential for the APS/sulfite redox couple is ~−60 mV, highlighting the limited driving force available from menaquinol alone (Eo′ ~ −75 mV) to power APS reduction and the likely need for coupling mechanisms (2014 synthesis; ARM Ramos work) (ramos2014studyofnovel pages 196-199).

4) Interactions and pathway context in D. vulgaris Hildenborough
- Direct interaction with QmoABC: Multiple orthogonal methods (pull-down, co-IP, Far-Western, crosslinking, and SPR) demonstrated that D. vulgaris QmoABC directly interacts with AprAB, with a measured steady-state affinity KD = 90 ± 3 nM and transient complex behavior dominated by fast dissociation. QmoA is the principal subunit mediating contact with AprAB (Frontiers in Microbiology, 2012; https://doi.org/10.3389/fmicb.2012.00137) (ramos2012themembraneqmoabc pages 1-2, ramos2012themembraneqmoabc pages 3-4, ramos2014studyofnovel pages 172-176).
- Electron donor problem and proposed solutions: In vitro assays with purified components did not detect electron transfer from menaquinol analogs through QmoABC to AprAB, leading to proposals that a third partner enables reverse electron bifurcation/confurcation to provide the necessary driving force. Candidate low-potential partners include ferredoxin, hydrogenase, or formate dehydrogenase feeding electrons into a flavin-based coupling center on Qmo, consistent with homology to bifurcating enzyme families (2014 synthesis and analysis referencing Desulfovibrio systems) (ramos2014studyofnovel pages 196-199, ramos2014studyofnovel pages 172-176).
- Gene clustering and co-occurrence: aprBA frequently co-localizes with qmoABC in SRP genomes, and phylogeny distinguishes Apr lineages that differ in associated electron transfer modules (e.g., Qmo vs AprM), supporting a conserved functional linkage between Apr and membrane redox complexes in Desulfovibrio (Microbiology, 2007; PLoS ONE, 2008; https://doi.org/10.1099/mic.0.2006/003152-0; https://doi.org/10.1371/journal.pone.0001514) (meyer2007phylogenyofthe pages 1-2, meyer2008homologymodelingof pages 1-2).

5) Cellular localization and complex organization
- Localization: AprAB (including AprB) is soluble/cytoplasmic but operates in proximity to the inner membrane via transient interactions with QmoABC during electron transfer. AprAB itself is not a membrane protein, whereas QmoC is a membrane subunit harboring heme b groups; QmoA/B are cytoplasmic and redox-active (Frontiers in Microbiology, 2012; https://doi.org/10.3389/fmicb.2012.00137) (ramos2012themembraneqmoabc pages 1-2).
- Broader electron-transfer network: In D. vulgaris, the electrogenic Qrc redox loop (H+/e− = 1) couples periplasmic and cytoplasmic redox pools, situating Qmo–AprAB within a larger energy-conserving electron-transport architecture central to sulfate respiration (Nature Communications, 2018; https://doi.org/10.1038/s41467-018-07839-x) ().

6) Structural/phylogenetic insights, domain architecture, and marker gene use
- Domain architecture: AprB consists of an Fe–S protein fold that accommodates two [4Fe–4S] centers, while AprA contains distinct FAD-binding and capping domains. Homology models across SRP and SOB show the catalytic vicinity around the FAD and Fe–S clusters is highly conserved, supporting a shared mechanism across lineages (PLoS ONE, 2008; https://doi.org/10.1371/journal.pone.0001514) (meyer2008homologymodelingof pages 1-2).
- Phylogeny and marker gene: aprBA (including aprB) phylogenies reveal at least two major lineages and instances of lateral gene transfer; apr genes are widely used as functional markers to survey sulfur cycling organisms in natural ecosystems, with demonstrated utility in freshwater lakes and other habitats (Microbiology, 2007; Scientific Reports, 2016; https://doi.org/10.1099/mic.0.2006/003152-0; https://doi.org/10.1038/srep36262) (meyer2007phylogenyofthe pages 1-2, ramos2012themembraneqmoabc pages 3-4).

7) Quantitative statistics and data
- Binding affinity: QmoABC–AprAB interaction KD = 90 ± 3 nM by SPR, demonstrating strong but transient association (Frontiers in Microbiology, 2012; https://doi.org/10.3389/fmicb.2012.00137) (ramos2012themembraneqmoabc pages 1-2, ramos2014studyofnovel pages 172-176).
- Enzymatic activity: Purified AprAB displayed sulfite oxidation activity of 3.3 µmol min−1 mg−1 in vitro under the reported assay conditions, evidencing catalytic competence and reversibility under certain conditions (Frontiers in Microbiology, 2012; https://doi.org/10.3389/fmicb.2012.00137) (ramos2012themembraneqmoabc pages 1-2, ramos2014studyofnovel pages 172-176).
- Redox loop stoichiometry: QrcABCD in D. vulgaris operates with an H+/e− ratio of 1, informing models for coupling of quinone cycling to cytoplasmic reductases, including AprAB (Nature Communications, 2018; https://doi.org/10.1038/s41467-018-07839-x) ().
- Thermodynamics: The APS/sulfite redox couple’s midpoint potential is ~−60 mV, indicating the need for coupling mechanisms (e.g., reverse electron bifurcation/confurcation) when driven by menaquinol alone (2014 synthesis) (ramos2014studyofnovel pages 196-199).

8) Current applications and real-world implementations
- Environmental marker and monitoring: aprBA (including aprB) is widely used as a functional marker to identify and classify sulfur-cycle prokaryotes in environmental surveys, enabling ecosystem-level assessments of sulfate reduction and sulfur oxidation potential (Scientific Reports, 2016; https://doi.org/10.1038/srep36262) (ramos2012themembraneqmoabc pages 3-4).
- Metabolic modeling and systems biology: Constraint-based and systems-level studies of Desulfovibrio integrate AprAB and associated redox complexes to capture metabolic versatility and energy conservation features, supporting industrial and environmental applications (Environmental Microbiology Reports, 2018; https://doi.org/10.1111/1758-2229.12619) ().

9) Expert opinions and synthesis
- Consensus view: Across authoritative reviews and comparative analyses, AprB is consistently assigned as the Fe–S electron-transfer subunit of APS reductase, relaying electrons between cytoplasmic redox partners (often via Qmo) and the catalytic FAD in AprA. Co-localization of aprBA with qmoABC and direct biophysical interaction support a conserved module in Desulfovibrio. While in vitro reconstitution of quinol-to-APS electron flow has remained challenging, genetic, biochemical, and thermodynamic considerations favor a role for additional low-potential partners and/or confurcation at Qmo to power APS reduction in vivo (Microbiology, 2007; PLoS ONE, 2008; Frontiers in Microbiology, 2012; ARM Ramos synthesis 2014) (meyer2007phylogenyofthe pages 1-2, meyer2008homologymodelingof pages 1-2, ramos2012themembraneqmoabc pages 1-2, ramos2014studyofnovel pages 196-199, ramos2014studyofnovel pages 172-176).

Limitations and gaps
- Recent AprB-specific structural biochemistry in D. vulgaris Hildenborough (2023–2024) is limited in the accessible literature; however, recent systems analyses emphasize the centrality of Qmo–AprAB in SRB energetics and encourage investigation of confurcating electron flow and partner proteins in vivo (Frontiers in Microbiology, 2023) (ramos2014studyofnovel pages 134-139).

References with URLs and publication dates
- Meyer, B. & Kuever, J. 2007. Microbiology (July 2007). Phylogeny of AprA/AprB; conserved heterodimer; pathway context. URL: https://doi.org/10.1099/mic.0.2006/003152-0 (meyer2007phylogenyofthe pages 1-2).
- Meyer, B. & Kuever, J. 2008. PLoS ONE (January 2008). Homology models of AprBA; conserved AprB 4Fe–4S architecture; Qmo linkage. URL: https://doi.org/10.1371/journal.pone.0001514 (meyer2008homologymodelingof pages 1-2).
- Ramos, A.R. et al. 2012. Frontiers in Microbiology (March 2012). Direct Qmo–AprAB interaction; KD; localization; complex composition. URL: https://doi.org/10.3389/fmicb.2012.00137 (ramos2012themembraneqmoabc pages 1-2, ramos2012themembraneqmoabc pages 3-4, ramos2014studyofnovel pages 172-176).
- Ramos, A.R.M. 2014 (synthesis). Energetic constraints; midpoint potentials; bifurcation/confurcation hypotheses in Desulfovibrio. Accessible via institutional repositories where available (ARM Ramos thesis/compilation) (ramos2014studyofnovel pages 196-199, ramos2014studyofnovel pages 172-176, ramos2014studyofnovel pages 134-139).
- Duarte, A.G. et al. 2018. Nature Communications (December 2018). Qrc electrogenic redox loop in D. vulgaris; H+/e− = 1. URL: https://doi.org/10.1038/s41467-018-07839-x ().
- Watanabe, T. et al. 2016. Scientific Reports (November 2016). aprBA as functional marker; lineage insights. URL: https://doi.org/10.1038/srep36262 (ramos2012themembraneqmoabc pages 3-4).
- Flowers, J.J. et al. 2018. Environmental Microbiology Reports (April 2018). Constraint-based modeling of D. vulgaris metabolism (context for integrating AprAB). URL: https://doi.org/10.1111/1758-2229.12619 ().
- Saxena, P. et al. 2023. Frontiers in Microbiology (April 2023). Systems integration highlighting essential sulfate-reduction genes and Qmo’s role. URL: https://doi.org/10.3389/fmicb.2023.1086021 (ramos2014studyofnovel pages 134-139).

References

1. (meyer2007phylogenyofthe pages 1-2): Birte. Meyer and Jan Kuever. Phylogeny of the alpha and beta subunits of the dissimilatory adenosine-5'-phosphosulfate (aps) reductase from sulfate-reducing prokaryotes–origin and evolution of the dissimilatory sulfate-reduction pathway. Microbiology, 153 Pt 7:2026-44, Jul 2007. URL: https://doi.org/10.1099/mic.0.2006/003152-0, doi:10.1099/mic.0.2006/003152-0. This article has 261 citations and is from a peer-reviewed journal.

2. (meyer2008homologymodelingof pages 1-2): Birte Meyer and Jan Kuever. Homology modeling of dissimilatory aps reductases (aprba) of sulfur-oxidizing and sulfate-reducing prokaryotes. PLoS ONE, 3:e1514, Jan 2008. URL: https://doi.org/10.1371/journal.pone.0001514, doi:10.1371/journal.pone.0001514. This article has 51 citations and is from a peer-reviewed journal.

3. (ramos2012themembraneqmoabc pages 1-2): Ana Raquel Ramos, K. Keller, J. Wall, and I. Pereira. The membrane qmoabc complex interacts directly with the dissimilatory adenosine 5′-phosphosulfate reductase in sulfate reducing bacteria. Frontiers in Microbiology, Mar 2012. URL: https://doi.org/10.3389/fmicb.2012.00137, doi:10.3389/fmicb.2012.00137. This article has 133 citations and is from a poor quality or predatory journal.

4. (ramos2014studyofnovel pages 134-139): ARM Ramos. Study of novel energy metabolism pathways in anaerobic bacteria. Unknown journal, 2014.

5. (ramos2012themembraneqmoabc pages 3-4): Ana Raquel Ramos, K. Keller, J. Wall, and I. Pereira. The membrane qmoabc complex interacts directly with the dissimilatory adenosine 5′-phosphosulfate reductase in sulfate reducing bacteria. Frontiers in Microbiology, Mar 2012. URL: https://doi.org/10.3389/fmicb.2012.00137, doi:10.3389/fmicb.2012.00137. This article has 133 citations and is from a poor quality or predatory journal.

6. (cadby2014theregulationof pages 21-25): IT Cadby. The regulation of gene expression in sulphate reducing bacteria. Unknown journal, 2014.

7. (ramos2014studyofnovel pages 196-199): ARM Ramos. Study of novel energy metabolism pathways in anaerobic bacteria. Unknown journal, 2014.

8. (ramos2014studyofnovel pages 172-176): ARM Ramos. Study of novel energy metabolism pathways in anaerobic bacteria. Unknown journal, 2014.

Citations

1. meyer2008homologymodelingof pages 1-2
2. ramos2012themembraneqmoabc pages 1-2
3. ramos2014studyofnovel pages 134-139
4. ramos2012themembraneqmoabc pages 3-4
5. cadby2014theregulationof pages 21-25
6. ramos2014studyofnovel pages 196-199
7. meyer2007phylogenyofthe pages 1-2
8. ramos2014studyofnovel pages 172-176
9. 4Fe–4S
10. https://doi.org/10.1099/mic.0.2006/003152-0;
11. https://doi.org/10.1371/journal.pone.0001514
12. https://doi.org/10.3389/fmicb.2012.00137
13. https://doi.org/10.3389/fmicb.2023.1086021
14. https://doi.org/10.1038/s41467-018-07839-x
15. https://doi.org/10.1038/srep36262
16. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.662646,
17. https://doi.org/10.1111/1758-2229.12619
18. https://doi.org/10.1099/mic.0.2006/003152-0
19. https://doi.org/10.1099/mic.0.2006/003152-0,
20. https://doi.org/10.1371/journal.pone.0001514,
21. https://doi.org/10.3389/fmicb.2012.00137,