Synthesis and Characterization of a Linear Dinitrosyl-Triiron Complex; Comparison to a Flavodiiron Nitric Oxide Reductase Intermediate
Name
Lippard_Synthesis with SI.pdf
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6.61 MB
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Checksum (MD5)
6535fc332aa7fc31a3bf9ae5392b76f9
Author(s)
Victor, Eric
Minier, Mikael Antoine
Lippard, Stephen J.
Alternative Title
Synthesis and Characterization of a Linear Dinitrosyl-Triiron Complex
Date Issued
June 2014
Journal
European Journal of Inorganic Chemistry
Publisher
Wiley Blackwell
Citation
Victor, Eric, Mikael A. Minier, and Stephen J. Lippard. “Synthesis and Characterization of a Linear Dinitrosyl-Triiron Complex.” European Journal of Inorganic Chemistry 2014.33 (2014): 5640–5645.
Version
Author's final manuscript
Abstract
Nitric oxide is released during the immune response by the host during bacterial infection. To counteract this response, bacteria have evolved nitric oxide reductases to convert NO to N[subscript 2]O. Some of these nitric oxide reductases contain a flavodiiron active site that has bridging carboxylates and hydroxides. Only a handful of synthetic complexes currently exist as models for the protein reactivity. Here, we report the reaction of [Fe[subscript 2](μ-OH)(μ-Ph[subscript 4]DBA)(TMEDA)[subscript 2](OTf)] (4) with NO(g) and Ph[subscript 3]CSNO to prepare the dinitrosyl-triiron complex [Fe[subscript 3](μ-OH)[subscript 2](μ-Ph[subscript 4]DBA)[subscript 2](TMEDA)[subscript 2](NO)[subscript 2]](OTf) (5). The reaction was monitored by UV/Vis and ReactIR spectroscopy, and compound 5 was characterized by X-ray crystallography, [superscript 57]Fe Mossbauer spectroscopy, Evan's method, and FTIR spectroscopy. The IR spectrum of compound 5 compares favorably to experimental spectroscopic data obtained for the proposed mononitrosylated intermediate of the protein.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1002/ejic.201402543
