ArticleThe Plant journal : for cell and molecular biology2015
Leghemoglobin is nitrated in functional legume nodules in a tyrosine residue within the heme cavity by a nitrite/peroxide-dependent mechanism.
Article in The Plant journal : for cell and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
- Rhizobia bacteroid transcription helps to coordinate the soybean nodule drought response.AoB PLANTS · 2026Article
- Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense againstFrontiers in plant science · 2026Article
- Persulfidation of plant and bacteroid proteins is involved in legume nodule development and senescence.Journal of experimental botany · 2024Article
- Dynamics of hemoglobins during nodule development, nitrate response, and dark stress in Lotus japonicus.Journal of experimental botany · 2024Article
- Functions of nitric oxide-mediated post-translational modifications under abiotic stress.Frontiers in plant science · 2023Review
- Signaling by reactive molecules and antioxidants in legume nodules.The New phytologist · 2022Review
- Protein Tyrosine Nitration in Plant Nitric Oxide Signaling.Frontiers in plant science · 2022Review
- Redox post-translational modifications and their interplay in plant abiotic stress tolerance.Frontiers in plant science · 2022Review
- Molecular responses of legumes to abiotic stress: post-translational modifications of proteins and redox signaling.Journal of experimental botany · 2021Review
- Nitric oxide function during oxygen deprivation in physiological and stress processes.Journal of experimental botany · 2021Review
- Tyrosine Nitration of Flagellins: a Response of Sinorhizobium meliloti to Nitrosative Stress.Applied and environmental microbiology · 2020Article
- Excess nitrate induces nodule greening and reduces transcript and protein expression levels of soybean leghaemoglobins.Annals of botany · 2020Article
- The Role of Nitric Oxide in Nitrogen Fixation by Legumes.Frontiers in plant science · 2020Review
- Plant Nitrate Reductases Regulate Nitric Oxide Production and Nitrogen-Fixing Metabolism During theFrontiers in plant science · 2020Article
- Nitric oxide molecular targets: reprogramming plant development upon stress.Journal of experimental botany · 2019Review
- Protein Carbonylation and Glycation in Legume Nodules.Plant physiology · 2018Article
- Redefining nitric oxide production in legume nodules through complementary insights from electron paramagnetic resonance spectroscopy and specific fluorescent probes.Journal of experimental botany · 2018Article
- RNA and mRNA Nitration as a Novel Metabolic Link in Potato Immune Response toFrontiers in plant science · 2018Article
- MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress inFrontiers in plant science · 2018Article
- Tyrosine-Nitrated Proteins: Proteomic and Bioanalytical Aspects.Antioxidants & redox signaling · 2017Review
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
Protein tyrosine (Tyr) nitration is a post-translational modification yielding 3-nitrotyrosine (NO2 -Tyr). Formation of NO2 -Tyr is generally considered as a marker of nitro-oxidative stress and is involved in some human pathophysiological disorders, but has been poorly studied in plants. Leghemoglobin (Lb) is an abundant hemeprotein of legume nodules that plays an essential role as an O2 transporter. Liquid chromatography coupled to tandem mass spectrometry was used for a targeted search and quantification of NO2 -Tyr in Lb. For all Lbs examined, Tyr30, located in the distal heme pocket, is the major target of nitration. Lower amounts were found for NO2 -Tyr25 and NO2 -Tyr133. Nitrated Lb and other as yet unidentified nitrated proteins were also detected in nodules of plants not receiving NO3- and were found to decrease during senescence. This demonstrates formation of nitric oxide (˙NO) and NO2- by alternative means to nitrate reductase, probably via a ˙NO synthase-like enzyme, and strongly suggests that nitrated proteins perform biological functions and are not merely metabolic byproducts. In vitro assays with purified Lb revealed that Tyr nitration requires NO2- + H2 O2 and that peroxynitrite is not an efficient inducer of nitration, probably because Lb isomerizes it to NO3-. Nitrated Lb is formed via oxoferryl Lb, which generates nitrogen dioxide and tyrosyl radicals. This mechanism is distinctly different from that involved in heme nitration. Formation of NO2 -Tyr in Lb is a consequence of active metabolism in functional nodules, where Lb may act as a sink of toxic peroxynitrite and may play a protective role in the symbiosis.
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