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Department of Applied Biosciences, College of Agriculture and Life Sciences, Kyungpook National University, Daegu 41566, Republic of Korea.

Nitrogen fixation in legume nodules is crucial for plant growth and development. Therefore, this study aims to investigate the effects of nitric oxide [S-nitrosoglutathione (GSNO)] and silicon [sodium metasilicate (Si)], both individually and in combination, on soybean growth, nodule formation, leghaemoglobin (Lb) synthesis, and potential post-translational modifications. At the V1 stage, soybean plants were treated for 2 weeks with 150 µM GSNO, and Si at concentrations of 1 mM, 2 mM, and 4 mM.

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A key feature in the establishment of symbiosis between plants and microbes is the maintenance of the balance between the production of the small redox-related molecule, nitric oxide (NO), and its cognate scavenging pathways. During the establishment of symbiosis, a transition from a normoxic to a microoxic environment often takes place, triggering the production of NO from nitrite via a reductive production pathway. Plant hemoglobins [phytoglobins (Phytogbs)] are a central tenant of NO scavenging, with NO homeostasis maintained via the Phytogb-NO cycle.

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Heme catabolism mediated by heme oxygenase in uninfected interstitial cells enables efficient symbiotic nitrogen fixation in Lotus japonicus nodules.

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Article Synopsis
  • Legume nodules make a lot of heme, which is important for creating leghemoglobin that helps plants fix nitrogen.
  • Scientists studied a plant called Lotus japonicus to find out how a specific enzyme called LjHO1 helps break down heme and discovered that this enzyme is crucial for keeping the plant healthy and fixing nitrogen.
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Protein folding is essential for a polypeptide chain to acquire its proper structure and function. Globins are a superfamily of ubiquitous heme-binding α-helical proteins whose function is principally to regulate oxygen homoeostasis. In this review, we explore the hierarchical helical formation in the globin proteins apomyoglobin and leghemoglobin, and we discuss the existence of non-native and misfolded structures occurring during the course of folding to its native state.

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