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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The symbol LBA is ambiguous across biology, but the research summarized here is restricted to the UniProt-defined target: UniProt P02234, described as leghemoglobin alpha / Leghemoglobin A (PvLba) from common bean (Phaseolus vulgaris) and belonging to the plant globin (leghemoglobin-like) family. A Phaseolus-specific primary study explicitly refers to “bean Lba (PvLba)” in functional bean nodules and measures its in vivo post-translational modification, supporting that the literature discussed here is on the correct protein identity (PvLba/leghemoglobin A), not an unrelated “LBA” in other taxa. (sainz2015leghemoglobinisnitrated pages 4-6)
Leghemoglobins (Lbs) are heme-containing globins that accumulate to very high levels in legume root nodules and are central to the physiology of symbiotic nitrogen fixation. In functional nodules, Lb is described as an abundant hemeprotein (reported in the millimolar range) whose essential biochemical function is oxygen (O₂) transport/delivery to the symbiosome/respiring nodule tissues while maintaining low free O₂ compatible with oxygen-labile nitrogenase. (sainz2015leghemoglobinisnitrated pages 1-3)
In P. vulgaris nodules specifically, PvLba is treated as the major bean leghemoglobin species in a Phaseolus-focused biochemical study, consistent with UniProt P02234 being a nodule hemoglobin. (sainz2015leghemoglobinisnitrated pages 1-3, sainz2015leghemoglobinisnitrated pages 4-6)
A defining mechanistic point is that only ferrous (Fe²⁺) leghemoglobin binds O₂, so maintenance of the reduced state is integral to function. (sainz2015leghemoglobinisnitrated pages 1-3)
Recent legume work synthesizes the physiological framing: Lb maintains a microoxic environment necessary for nitrogenase while still enabling respiration; free O₂ in infected nodule tissues has been described at nanomolar levels (<50 nM) in modern summaries of nodule physiology. (lamoureux2024theeffectof pages 26-29)
A current consensus view (supported by both Phaseolus primary work and recent legume genetics) is that Lbs are not only O₂ buffers but also intersect strongly with reactive nitrogen species (RNS) and reactive oxygen species (ROS):
A key Phaseolus-specific primary study demonstrated that PvLba is nitrated in functional bean nodules at a tyrosine residue within the heme cavity, with Tyr30 in the distal heme pocket being the predominant nitration site used for quantification. (sainz2015leghemoglobinisnitrated pages 4-6, sainz2015leghemoglobinisnitrated pages 1-3)
Quantitative in vivo observation: in young bean nodules, the fraction of PvLba nitrated at Tyr30 was approximately 0.23%, and nitration decreased in senescent nodules and after nitrate treatment; this is shown in the paper’s quantification figure. (sainz2015leghemoglobinisnitrated media 99e0ea56)
Mechanistic in vitro support (physiology-linked conditions): PvLba nitration required nitrite + hydrogen peroxide (H₂O₂), and was inhibited by iron chelation or scavengers of nitrating radicals, supporting a nitrite/peroxide-dependent mechanism coupled to heme redox chemistry. The study used conditions described as physiologically relevant (e.g., ferric Lb ~10 µM; H₂O₂ 20–100 µM; nitrite ~100 µM) to generate substantial nitration in vitro, whereas omission of H₂O₂ prevented nitration. (sainz2015leghemoglobinisnitrated pages 4-6)
Functional interpretation (author analysis): the authors suggest Lb can act as a sink for toxic reactive nitrogen/oxygen species (e.g., peroxynitrite-related chemistry), tying a Phaseolus leghemoglobin directly to nodule nitro-oxidative chemistry beyond oxygen transport. (sainz2015leghemoglobinisnitrated pages 1-3)
A 2024 Journal of Experimental Botany study in Lotus japonicus systematically quantified regulation of nodule hemoglobins and used CRISPR mutants lacking Lbs plus transcription-factor mutants. Major findings relevant to functional annotation of PvLba by homology/conservation include:
Although these experiments are not in P. vulgaris, they represent authoritative, modern functional genetics supporting a conserved role of Lbs (including PvLba) in balancing O₂ supply with redox/NO constraints in nodules. (minguillon2024dynamicsofhemoglobins pages 1-2)
A 2024 review in Plant Communications emphasizes:
This consolidates expert-level interpretation that Lb status is tightly linked to both symbiotic performance and nodule lifespan/turnover. (berrabah2024defenseandsenescence pages 1-2)
A 2024 Frontiers in Plant Science transcriptome/anatomy study in soybean–rhizobium combinations reports enrichment and higher expression of oxygen-binding genes (including oxygen-binding proteins such as leghemoglobin) in conditions associated with effective/fully developed nodules, consistent with Lb-mediated microoxia being a central determinant of symbiotic effectiveness. (zadegan2024differentialsymbioticcompatibilities pages 11-12)
Based on Phaseolus-specific biochemistry and cross-legume consensus:
Within the available evidence, Lb is consistently described as nodule-localized and functioning in the infected nodule environment where symbiosomes and nitrogenase activity occur; its function is explicitly tied to delivering O₂ to the symbiosomal membrane and maintaining microoxic conditions. (lamoureux2024theeffectof pages 26-29)
PvLba itself is a bean nodule protein, but the broader leghemoglobin protein class has a major real-world deployment as a color/flavor heme ingredient in plant-based meat analogues, enabled by precision fermentation.
EFSA’s 2024 scientific opinion evaluated soy leghemoglobin produced in genetically modified Komagataella phaffii (LegH Prep) for use as a colouring in meat analogue products and concluded that it does not raise a safety concern at proposed use and use levels. (younes2024safetyofsoy pages 4-6, younes2024safetyofsoy pages 1-2)
Key quantitative statistics from EFSA’s exposure/safety evaluation include:
These regulatory documents provide authoritative, real-world implementation context for leghemoglobin proteins as ingredients, even though they pertain to soybean leghemoglobin rather than PvLba from bean. (younes2024safetyofsoy pages 3-4, younes2024safetyofsoy pages 4-6)
Recent biotechnology literature reports strong progress in recombinant leghemoglobin production:
Across recent authoritative sources, the expert framing of Lb biology converges on:
PvLba (UniProt P02234; gene LBA) is a nodule-localized leghemoglobin that binds O₂ via a heme cofactor (ferrous state) and supports symbiotic nitrogen fixation by buffering and delivering O₂ at very low free concentrations compatible with nitrogenase. PvLba also participates in nodule redox/RNS chemistry: it forms NO-bound complexes and undergoes measurable in vivo tyrosine nitration (primarily Tyr30 in the distal heme pocket) via a nitrite/peroxide-dependent mechanism, linking it to NO/ROS homeostasis in functional nodules. (sainz2015leghemoglobinisnitrated pages 1-3, sainz2015leghemoglobinisnitrated pages 4-6, sainz2015leghemoglobinisnitrated media 99e0ea56)
| Functional aspect | Key statements | Evidence type | Quantitative data | Key references with year and DOI URL | PaperQA citation IDs |
|---|---|---|---|---|---|
| O2 transport/buffering | PvLba is a highly abundant nodule hemeprotein whose essential role is O2 transport/delivery to symbiosomes while buffering free O2 to protect nitrogenase. Closely related leghemoglobins in legumes occur at millimolar concentrations and help maintain very low free O2 in infected cells. | Primary; review | Lb abundance in nodules ~1–5 mM; free O2 reported as <50 nM in nodules in recent legume literature. | Sainz et al., 2015, Plant J. DOI: https://doi.org/10.1111/tpj.12762; Minguillón et al., 2024, J Exp Bot DOI: https://doi.org/10.1093/jxb/erad455 | (sainz2015leghemoglobinisnitrated pages 1-3, minguillon2024dynamicsofhemoglobins pages 1-2, lamoureux2024theeffectof pages 26-29) |
| NO/ROS chemistry | PvLba reacts with reactive nitrogen/oxygen species; ferrous Lb binds NO to form LbNO, and Lbs can convert NO-derived species to nitrate in vitro. Recent mutant data in Lotus indicate that loss of Lbs causes NO and ROS accumulation, supporting a conserved role in nodule redox homeostasis. | Primary; review | In vitro PvLba nitration assays used ~10 µM ferric Lb, 20–100 µM H2O2, and ~100 µM nitrite; nitrate treatments in Lotus study were 0, 0.5, 5, 10 mM KNO3 for 2 d. | Sainz et al., 2015, https://doi.org/10.1111/tpj.12762; Minguillón et al., 2024, https://doi.org/10.1093/jxb/erad455 | (sainz2015leghemoglobinisnitrated pages 4-6, sainz2015leghemoglobinisnitrated pages 1-3, minguillon2024dynamicsofhemoglobins pages 1-2, minguillon2024dynamicsofhemoglobins pages 13-15, minguillon2024dynamicsofhemoglobins pages 16-17) |
| Post-translational modifications | PvLba is nitrated in functional bean nodules, predominantly at Tyr30 in the distal heme pocket, indicating in vivo modification by nitrite/peroxide chemistry. This supports that LBA is an active redox-reactive globin in nodules rather than a passive O2 carrier only. | Primary | Young bean nodules contained ~0.23% nitrated PvLba; in vitro nitration reached ~25–70% under tested oxidant/nitrite conditions; nitration decreased in senescent and nitrate-treated nodules. | Sainz et al., 2015, https://doi.org/10.1111/tpj.12762 | (sainz2015leghemoglobinisnitrated pages 4-6, sainz2015leghemoglobinisnitrated media 99e0ea56) |
| Regulation by nitrate/stress | Recent legume data show Lb genes are strongly down-regulated by nitrate and dark stress, with nitrate-responsive promoter elements implicated. This is relevant to PvLba annotation because leghemoglobin expression is tightly coupled to nodule physiological state and N-fixation activity. | Primary | Nitrate suppressed Lbs after 2 d exposure to 0.5–10 mM KNO3; compensatory regulation between Lb paralogs was observed in Lotus mutants. | Minguillón et al., 2024, https://doi.org/10.1093/jxb/erad455 | (minguillon2024dynamicsofhemoglobins pages 1-2, minguillon2024dynamicsofhemoglobins pages 13-15, minguillon2024dynamicsofhemoglobins pages 16-17, minguillon2024dynamicsofhemoglobins pages 17-18) |
| Role in senescence/defense | Leghemoglobin is a marker of functional pink nodules; oxidation/decrease of Lb accompanies senescence and loss of N-fixation capacity. Reviews and recent studies connect Lb decline with nitro-oxidative stress, defense activation, and senescence-associated changes in antioxidants and proteolysis. | Review; primary | Nodule N2-fixation peak ~4 weeks and lifespan ~10–12 weeks in a recent synthesis; antioxidants in nodules include ascorbate ~1–2 mM and glutathione ~0.5–1 mM; APX ~0.9% of soluble protein. | Berrabah et al., 2024, Plant Commun. DOI: https://doi.org/10.1016/j.xplc.2024.100888; Minguillón et al., 2024, https://doi.org/10.1093/jxb/erad455 | (berrabah2024defenseandsenescence pages 1-2, lamoureux2024theeffectof pages 26-29, minguillon2024dynamicsofhemoglobins pages 13-15, lamoureux2024theeffectof pages 29-32) |
| Applications in food/fermentation | Although not specific to PvLba from bean, closely related leghemoglobins are used as heme/flavor-color ingredients in plant-based meat and are being optimized by precision fermentation in yeasts. Recent biotech studies report substantially improved recombinant production titers. | Biotech; review | K. marxianus intracellular LBA reached 7.27 g/L in 5 L fermentor with heme content 66.32 mg/L; S. cerevisiae intracellular LegH reached 544.8 mg/L and secreted LegH 88.5 mg/L; another K. phaffii process reported highest biomass density 121.80 gDCW/L and LegH yield 0.513 mg/gDCW. | Tian et al., 2024, Front Bioeng Biotechnol. DOI: https://doi.org/10.3389/fbioe.2023.1329016; Huang et al., 2024, Fermentation DOI: https://doi.org/10.3390/fermentation10030146; Suleiko et al., 2024, Fermentation DOI: https://doi.org/10.3390/fermentation10010055 | (tian2024highlevelexpressionof pages 1-2, huang2024efficientsecretoryexpression pages 1-2) |
| Safety/exposure data | Regulatory assessments of soy leghemoglobin produced in GM yeast concluded no safety concern at proposed use levels in meat analogues, though these data apply to soy LegH rather than bean PvLba directly. The evidence is still useful for real-world implementation of the leghemoglobin protein class. | Regulatory | Proposed maximum use level 0.8% soy leghemoglobin protein in meat analogues; mean dietary exposure up to 7.3 mg/kg bw/day and 95th percentile up to 32.9 mg/kg bw/day; NOAEL in 90-day study at highest tested doses corresponded to 2328 mg/kg bw/day (males) and 2865 mg/kg bw/day (females) soy leghemoglobin. | Younes et al., 2024, EFSA J. DOI: https://doi.org/10.2903/j.efsa.2024.8822; Casacuberta et al., 2024, EFSA J. DOI: https://doi.org/10.2903/j.efsa.2024.9060 | (younes2024safetyofsoy pages 3-4, younes2024safetyofsoy pages 4-6, casacuberta2024assessmentofsoy pages 10-11, younes2024safetyofsoy pages 1-2, casacuberta2024assessmentofsoy pages 12-12) |
Table: This table summarizes the functional annotation of Phaseolus vulgaris leghemoglobin A (PvLba; UniProt P02234) using direct bean evidence where available and closely related leghemoglobin evidence for conserved functions, regulation, applications, and safety context.
References
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(huang2024efficientsecretoryexpression pages 1-2): Yiyun Huang, Jingwen Zhou, Jianghua Li, Guocheng Du, Jian Chen, and Xinrui Zhao. Efficient secretory expression of leghemoglobin in saccharomyces cerevisiae. Fermentation, 10:146, Mar 2024. URL: https://doi.org/10.3390/fermentation10030146, doi:10.3390/fermentation10030146. This article has 9 citations.
(pentjuss2023pichiapastorisgrowth—coupled pages 4-5): Agris Pentjuss, Emils Bolmanis, Anastasija Suleiko, Elina Didrihsone, Arturs Suleiko, Konstantins Dubencovs, Janis Liepins, Andris Kazaks, and Juris Vanags. Pichia pastoris growth—coupled heme biosynthesis analysis using metabolic modelling. Scientific Reports, Sep 2023. URL: https://doi.org/10.1038/s41598-023-42865-w, doi:10.1038/s41598-023-42865-w. This article has 12 citations and is from a peer-reviewed journal.
(minguillon2024dynamicsofhemoglobins pages 16-17): Samuel Minguillón, Ángela Román, Carmen Pérez-Rontomé, Longlong Wang, Ping Xu, Jeremy D Murray, Deqiang Duanmu, Maria C Rubio, and Manuel Becana. Dynamics of hemoglobins during nodule development, nitrate response, and dark stress in lotus japonicus. Journal of Experimental Botany, 75:1547-1564, Nov 2024. URL: https://doi.org/10.1093/jxb/erad455, doi:10.1093/jxb/erad455. This article has 12 citations and is from a domain leading peer-reviewed journal.
(minguillon2024dynamicsofhemoglobins pages 17-18): Samuel Minguillón, Ángela Román, Carmen Pérez-Rontomé, Longlong Wang, Ping Xu, Jeremy D Murray, Deqiang Duanmu, Maria C Rubio, and Manuel Becana. Dynamics of hemoglobins during nodule development, nitrate response, and dark stress in lotus japonicus. Journal of Experimental Botany, 75:1547-1564, Nov 2024. URL: https://doi.org/10.1093/jxb/erad455, doi:10.1093/jxb/erad455. This article has 12 citations and is from a domain leading peer-reviewed journal.
(lamoureux2024theeffectof pages 29-32): KE Lamoureux. The effect of copper-induced oxidative stress on symbiosis between model legume lotus japonicus and mesorhizobium loti. Unknown journal, 2024.
(casacuberta2024assessmentofsoy pages 10-11): Josep Casacuberta, Francisco Barro, Albert Braeuning, Pilar Cubas, Ruud de Maagd, Michelle M. Epstein, Thomas Frenzel, Jean‐Luc Gallois, Frits Koning, Antoine Messéan, F. Javier Moreno, Fabien Nogué, Giovanni Savoini, Alan H. Schulman, Christoph Tebbe, Eve Veromann, Andrea Gennaro, Aina Belen Gil Gonzalez, José Ángel Gómez Ruiz, Tilemachos Goumperis, Dafni Maria Kagkli, Paolo Lenzi, Aleksandra Lewandowska, Pietro Piffanelli, and Reinhilde Schoonjans. Assessment of soy leghemoglobin produced from genetically modified komagataella phaffii, under regulation (ec) no 1829/2003 (application efsa‐gmo‐nl‐2019‐162). EFSA Journal, Nov 2024. URL: https://doi.org/10.2903/j.efsa.2024.9060, doi:10.2903/j.efsa.2024.9060. This article has 4 citations and is from a peer-reviewed journal.
(pentjuss2023pichiapastorisgrowth—coupled pages 1-2): Agris Pentjuss, Emils Bolmanis, Anastasija Suleiko, Elina Didrihsone, Arturs Suleiko, Konstantins Dubencovs, Janis Liepins, Andris Kazaks, and Juris Vanags. Pichia pastoris growth—coupled heme biosynthesis analysis using metabolic modelling. Scientific Reports, Sep 2023. URL: https://doi.org/10.1038/s41598-023-42865-w, doi:10.1038/s41598-023-42865-w. This article has 12 citations and is from a peer-reviewed journal.