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• W2328786093 abstract "The detoxification of nitric oxide (NO) by bacterial NO reductase (NorBC) has gained much attention as this reaction provides a paradigm as to how NO can be detoxified anaerobically in cells. However, a clear mechanistic picture of how the heme/non-heme active site of NorBC activates NO is lacking, mostly as a result of insufficient knowledge about the properties of the non-heme iron(II)-NO adduct. Here we report the first biomimetic model complexes for this species that closely resemble the coordination environment found in the protein, using the ligands BMPA-Pr and TPA. The systematic investigation of these compounds allowed us to gain key insight into the electronic structure and geometric properties of high-spin non-heme iron(II)-NO adducts. In particular, we show how small changes in the ligand environment of iron could be used by NorBC to greatly modulate the properties, and hence, the reactivity of this species." @default.
• W2328786093 created "2016-06-24" @default.
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• W2328786093 date "2011-10-26" @default.
• W2328786093 modified "2023-10-16" @default.
• W2328786093 title "Structural and electronic characterization of non-heme Fe(II)-nitrosyls as biomimetic models of the Fe(B) center of bacterial nitric oxide reductase." @default.
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• W2328786093 doi "https://doi.org/10.1021/ja111693f" @default.
• W2328786093 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21630658" @default.
• W2328786093 hasPublicationYear "2011" @default.
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