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Bacterial NO reductase (bacNOR) enzymes utilize a heme/non-heme active site to couple two NO molecules to N 2 O. We show that BF 3 coordination to the nitrosyl O-atom in (OEP)Fe(NO) activates it toward N-N bond formation with NO to generate N 2 O. 15 N-isotopic labeling reveals a reversible nitrosyl exchange reaction and follow-up N-O bond cleavage in the N 2 O formation step. Other Lewis acids (B(C 6 F 5 ) 3 and K + ) also promote the NO coupling reaction with (OEP)Fe(NO). These results, complemented by DFT calculations, provide experimental support for the cis: b 3 pathway in bacNOR.

Lewis Acid Activation of the Ferrous Heme–NO Fragment toward the N–N Coupling Reaction with NO To Generate N2O

Lewis Acid Activation of the Ferrous Heme–NO Fragment toward the N–N Coupling Reaction with NO To Generate N₂O