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Nickel (Ni) is a naturally occurring metal, but anthropogenic activities such as industrialization, use of fertilizers, chemicals, and sewage sludge have increased its concentration in the environment up to undesirable levels. Ni is considered to be essential for plant growth at low concentration; however, Ni pollution is increasing in the environment, and therefore, it is important to understand its functional roles and toxic effects on plants. This review emphasizes the environmental sources of Ni, its essentiality, effects, tolerance mechanisms, possible remediation approaches, and research direction that may help in interdisciplinary studies to assess the significance of Ni toxicity. Briefly, Ni affects plant growth both positively and negatively, depending on the concentration present in the growth medium. On the positive side, Ni is essential for normal growth, enzymatic activities (e.g., urease), nitrogen metabolism, iron uptake, and specific metabolic reactions. On the negative side, Ni reduces seed germination, root and shoot growth, biomass accumulation, and final production. Moreover, Ni toxicity also causes chlorosis and necrosis and inhibits various physiological processes (photosynthesis, transpiration) and cause oxidative damage in plants. The threat associated with Ni is increased as Ni concentration increases day by day in the environment, particularly in soils; therefore, it would be hazardous for crop production in the near future. Additionally, the lack of information regarding the mechanisms of Ni tolerance in plants further intensifies this situation. Therefore, future research should be focused on approachable and prominent solutions in order to minimize the entry of Ni into our ecosystems.

The aim of this study is to familiarize the Role of nickel in the Environment and in living organisms. This metal is widely used in many fields such as electrical engineering, medicine, Jewellery or Automotive Industry. Furthermore, it's an important part of our food. As the central atom of bacterial enzymes it participates in degradation of urea.. Nickel is also an micronutritient essential for proper functioning of the human body, as it increases hormonal activity and is involved in lipid metabolism. This metal makes it's way to the human body through respiratory tract, digestive system and skin. Large doses of nickel or prolonged contact with it could cause a variety of side effects. Harmfull effects of Nickel are genotoxicity haematotoxicity, teratogenicity, immunotoxicity and carcinogenicity. The population of people allergic to nickel is growing, it occcurs much more often to the women and it can appear in many way. Hypersensitivity to nickel can also be occupational. Due to the increasing prevalence of allergies to nickel. European regulations have been introduced to reduce the content of this metal in products of everyday usage. In countries which have fulfilled the above-mentioned law, the plunge of hypersensitivities has been observed., (© 2016 MEDPRESS.)

Crystal structures of nickel-dependent superoxide dismutases (NiSODs) reveal the presence of a H-bonding network formed between the NH group of the apical imidazole ligand from His1 and the Glu17 carboxylate from a neighboring subunit in the hexameric enzyme. This interaction is supported by another intrasubunit H-bond between Glu17 and Arg47. In this study, four mutant NiSOD proteins were produced to experimentally evaluate the roles of this H-bonding network and compare the results with prior predictions from density functional theory calculations. The X-ray crystal structure of H1A-NiSOD, which lacks the apical ligand entirely, reveals that in the absence of the Glu17-His1 H-bond, the active site is disordered. Characterization of this variant using X-ray absorption spectroscopy (XAS) shows that Ni(II) is bound in the expected N2S2 planar coordination site. Despite these structural perturbations, the H1A-NiSOD variant retains 4% of wild-type (WT) NiSOD activity. Three other mutations were designed to preserve the apical imidazole ligand but perturb the H-bonding network: R47A-NiSOD, which lacks the intramolecular H-bonding interaction; E17R/R47A-NiSOD, which retains the intramolecular H-bond but lacks the intermolecular Glu17-His1 H-bond; and E17A/R47A-NiSOD, which lacks both H-bonding interactions. These variants were characterized by a combination of techniques, including XAS to probe the nickel site structure, kinetic studies employing pulse-radiolytic production of superoxide, and electron paramagnetic resonance to assess the Ni redox activity. The results indicate that in addition to the roles in redox tuning suggested on the basis of previous computational studies, the Glu17-His1 H-bond plays an important structural role in the proper folding of the "Ni-hook" motif that is a critical feature of the active site.