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Abstract Some bacterial heme proteins catalyze the coupling of two NO molecules to generate N2O. We previously reported that a heme Fe–NO model engages in this N−N bond‐forming reaction with NO. We now demonstrate that (OEP)CoII(NO) similarly reacts with 1 equiv of NO in the presence of the Lewis acids BX3(X=F, C6F5) to generate N2O. DFT calculations support retention of the CoIIoxidation state for the experimentally observed adduct (OEP)CoII(NO⋅BF3), the presumed hyponitrite intermediate (P.+)CoII(ONNO⋅BF3), and the porphyrin π‐radical cation by‐product of this reaction, and that the π‐radical cation formation likely occurs at the hyponitrite stage. In contrast, the Fe analogue undergoes a ferrous‐to‐ferric oxidation state conversion during this reaction. Our work shows that cobalt hemes are chemically competent to engage in the NO‐to‐N2O conversion reaction.
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Insight into the preferential N-binding versus O-binding of nitrosoarenes to ferrous and ferric heme centers
Nitrosoarenes (ArNOs) are toxic metabolic intermediates that bind to heme proteins to inhibit their functions. Although much of their biological functions involve coordination to the Fe centers of hemes, the factors that determine N-binding or O-binding of these ArNOs have not been determined. We utilize X-ray crystallography and density functional theory (DFT) analyses of new representative ferrous and ferric ArNO compounds to provide the first theoretical insight into preferential N-binding versus O-binding of ArNOs to hemes. Our X-ray structural results favored N-binding of ArNO to ferrous heme centers, and O-binding to ferric hemes. Results of the DFT calculations rationalize this preferential binding on the basis of the energies of associated spin-states, and reveal that the dominant stabilization forces in the observed ferrous N-coordination and ferric O-coordination are dπ–pπ* and dσ–pπ*, respectively. Our results provide, for the first time, an explanation why in situ oxidation of the ferrous-ArNO compound to its ferric state results in the observed subsequent dissociation of the ligand.
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- Award ID(s):
- 1900181
- PAR ID:
- 10277002
- Date Published:
- Journal Name:
- Dalton Transactions
- Volume:
- 50
- Issue:
- 10
- ISSN:
- 1477-9226
- Page Range / eLocation ID:
- 3487 to 3498
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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Accepted Manuscript1.0
- Journal Article:
- https://doi.org/10.1039/d0dt03604h
