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Nitric oxide (NO) is an important molecule that regulates many physiological processes in humans and plants and contributes to the formation of greenhouse gases. Bacterial NO reductases utilize a di-Fe heme/nonheme active site to couple two NOs to generate nitrous oxide (N2O) via a two-electron mechanism. Here, we report a previously unexplored Cr porphyrin NO complex with a Lewis acid (LA) BF3 for the NO reduction reaction. Density functional theory calculations were first employed to reveal its reaction mechanism with a reasonable barrier for experimental realization. Subsequent experimental synthesis work confirms this reactivity and reports the first nitrosyl Cr porphyrin X-ray crystal structure. Theoretical analysis uncovered a distinctive reaction feature for the Cr system compared to Fe and Co porphyrins: the electron transfer from the metal to the bound NO occurs before LA binding. A comparative study of the NO coupling mechanisms with the three representative metals suggests that the metal reduction potential should be finely tuned, as found in previous studies of NOR enzymatic systems. Overall, this study offers new theoretical and experimental insights to further facilitate the development of alternative NO reduction compounds with biological, environmental, and industrial applications. 

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. 

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)Co^II(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 Co^IIoxidation state for the experimentally observed adduct (OEP)Co^II(NO⋅BF₃), the presumed hyponitrite intermediate (P^.+)Co^II(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.