Reversible Hydride Transfer to N,N'-Diarylimidazolinium Cations from Hydrogen Catalyzed by Transition Metal Complexes Mimicking the Reaction of [Fe]-Hydrogenase

Abstract

[Fe]-hydrogenase is a key enzyme involved in methanogenesis and facilitates reversible hydride transfer from H₂ to N⁵,N¹⁰-methenyltetrahydromethanopterin (CH-H₄MPT⁺). In this study, a reaction system was developed to model the enzymatic function of [Fe]-hydrogenase by using N,N'-diphenylimidazolinium cation (1⁺) as a structurally related alternative to CH-H₄MPT⁺. In connection with the enzymatic mechanism via heterolytic cleavage of H₂ at the single metal active site, several transition metal complex catalysts capable of such activation were utilized in the model system. Reduction of 1[BF₄] to N,N'-diphenylimidazolidine (2) was achieved under 1 atm H₂ at ambient temperature in the presence of an equimolar amount of NEt₃ as a proton acceptor. The proposed catalytic pathways involved the generation of active hydride complexes and subsequent intermolecular hydride transfer to 1⁺. The reverse reaction was accomplished by treatment of 2 with HNMe₂Ph⁺ as the proton source, where [(η⁵-C₅Me₅)Ir{(p-MeC₆H₄SO₂)NCHPhCHPhNH}] was found to catalyze the formation of 1⁺ and H₂ with high efficiency. These results are consistent with the fact that use of 2,6-lutidine in the forward reaction or 2,6-lutidinium in the reverse reaction resulted in incomplete conversion. By combining these reactions using the above Ir amido catalyst, the reversible hydride transfer interconverting 1⁺/H₂ and 2/H⁺ was performed successfully. This system demonstrated the hydride-accepting and hydride-donating modes of biologically relevant N-heterocycles coupled with proton concentration. The influence of substituents on the forward and reverse reactivities was examined for the derivatives of 1⁺ and 2 bearing one para-substituted N-phenyl group.