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系统地比较了FeMo-co和固氮酶的各种模拟体系在KBH_4还原乙炔为乙烯的反应中的催化活性和选择性。FeMo-co(活性:转变数为34;选择性:99％C_2H_4)和本实验室合成的模型化合物(活性:转变数为20～30;选择性;91～95％)比其它固氮酶的模拟体系(MoO_4~(2-)-CySH;MoO_4~(2-)—CySH—Fe~(2+);MoOS_4~(2-)—胰岛素;[Fe_4S_4(SCH_2Φ)_4]~(2-);和MoS_4~(2-))具有较高的活性和选择性;这可作为FeMo—co及其合成模拟物的原子簇活性中心多核络合活化底物分子的一种判据.
The catalytic activities and selectivities of various simulated systems of FeMo-co and nitrogenase were systematically compared in the KBH4 reduction of acetylene to ethylene. FeMo-co (activity: number of transitions: 34; selectivity: 99% C 2 H 4) and model compounds synthesized in our laboratory (activity: number of transitions 20-30; selectivity; 91-95% (MoO_4 ~ (2 -) - CySH; MoO_4 ~ (2 -) - CySH-Fe ~ (2 +); MoOS_4 ~ (2 -) - insulin; [Fe_4S_4 (SCH_2Φ) _4] ~ MoS_4 ~ (2-)) has high activity and selectivity; this can be used as a criterion for the activation of multi-core ligand-activated substrate molecules in the active centers of FeMo-co and its synthetic mimics.