A new oxidative pathway of nitric oxide production from oximes in plants.

Nitric oxide (NO) is an essential reactive oxygen species and a signal molecule in plants. Although several studies have proposed the occurrence of oxidative NO production, only reductive routes for NO production, such as the nitrate (NO-3) -upper-reductase pathway, have been evidenced to date in land plants. However, plants grown axenically with ammonium as the sole source of nitrogen exhibit contents of nitrite and NO, evidencing the existence of a metabolic pathway for oxidative production of NO.

Both Free Indole-3-Acetic Acid and Photosynthetic Performance are Important Players in the Response of Medicago truncatula to Urea and Ammonium Nutrition Under Axenic Conditions.

We aimed to identify the early stress response and plant performance of Medicago truncatula growing in axenic medium with ammonium or urea as the sole source of nitrogen, with respect to nitrate-based nutrition. Biomass measurements, auxin content analyses, root system architecture (RSA) response analyses, and physiological parameters were determined. Both ammonium and ureic nutrition severely affected the RSA, resulting in changes in the main elongation rate, lateral root development, and insert position from the root base.

Evaluation of the anti-nitrative effect of plant antioxidants using a cowpea Fe-superoxide dismutase as a target.

Nitric oxide cytotoxicity arises from its rapid conversion to peroxynitrite (ONOO(-)) in the presence of superoxide, provoking functional changes in proteins by nitration of tyrosine residues. The physiological significance of this post-translational modification is associated to tissue injury in animals, but has not been yet clarified in plants. The objective of this study was to establish new approaches that could help to understand ONOO(-) reactivity in plants.

Use of recombinant iron-superoxide dismutase as a marker of nitrative stress.

Superoxide dismutases (SODs; EC 1.15.1.

A self-induction method to produce high quantities of recombinant functional flavo-leghemoglobin reductase.

Ferric leghemoglobin reductase (FLbR) is able to reduce ferric leghemoglobin (Lb3+) to ferrous (Lb2+) form. This reaction makes Lb functional in performing its role since only reduced hemoglobins bind O2. FLbR contains FAD as prosthetic group to perform its activity.