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http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8932Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.advisor | SIL, DEBANGSU | - |
| dc.contributor.author | PANJA, ARIJIT | - |
| dc.date.accessioned | 2024-05-21T10:47:49Z | - |
| dc.date.available | 2024-05-21T10:47:49Z | - |
| dc.date.issued | 2024-05 | - |
| dc.identifier.citation | 43 | en_US |
| dc.identifier.uri | http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8932 | - |
| dc.description.abstract | In biological systems, different types of nitrite reductase (NiRs) and nitric oxide synthase (NOS) isozymes are present to generate NO for physiological activities. To mimic this function, we choose the acid-induced path to reduced nitrite for nickel-nitrite metal complexes. In this study, we utilized the (BimH)3 ligand framework and synthesized three different complexes, namely [(BimH)3NiII(μ-Cl)2NiII(BimH)3]Cl2 (1), [(BimH)3NiII(L1)(L2)][NO3]2 (2), and [(BimH)3NiII(κ2O2NO)](NO3) (3). These complexes are characterized by different methods such as 1H, ESI-MS, SCXRD, UV-Vis, FT-IR. 2 and 3 are used to synthesis a main precursor [(BimH)3NiII(κ2-ONO)][NO3] (4) complex. Acid induced reduction of 4 leads to detachment of nitrite from the nickel sites as evident from the disappearance of the nitrite band in the FTIR. ESI-MS spectra reveals the formation of 2,5-di-tert-butylcatechol which is an indirect evidence of the homolytic N-O bond cleavage upon protonation. | en_US |
| dc.language.iso | en | en_US |
| dc.subject | Bioinorganic Chemistry | en_US |
| dc.title | Synthesis, characterization, and nitrite reductase activity of Ni(II) complexes | en_US |
| dc.type | Thesis | en_US |
| dc.description.embargo | Two Years | en_US |
| dc.type.degree | MSc. | en_US |
| dc.contributor.department | Dept. of Chemistry | en_US |
| dc.contributor.registration | 20226214 | en_US |
| Appears in Collections: | MS THESES | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| 20226214_Arijit_Panja_MSc_Thesis.pdf | MS Thesis | 1.97 MB | Adobe PDF | View/Open |
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