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固氮酶及合成氨Fe催化剂中N2的络合位
N2-Binding Site in Nitrogenase and Ammonia Synthesis with Iron Catalysts
【摘要】 用乙烯为探针研究了固氮酶中N2的键合位。结果表明,乙烯不能与N2在固氮酶体系中相竞争。提出N2在固氮酶中的键合位很可能是蛋白键合FeMo-co笼内6Fe位的μ6(η2,ε4)和3Fe+1Mo位的μ4(η3,ε1)方式,而不是笼口2Fe位的μ2(η2)方式,在合成氨Fe催化剂中N2的络合方式可能是μ6(η3,ε3)。
【Abstract】 Ethylene was used as a probe to detect the N2-binding site in nitrogenase.It was found that ethylene couldn’t compete with N2 in the nitrogenase system.So the N2 binding site in nitrogenase might probably be the mode of 6Fe[μ6(η2,ε)]and the mode of 3Fe +1Mo[μ4(η3,ε1)] in the cage of the protein-bonded FeMo-co, but not be the mode of dinuclear coordination occurred on the 2Fe-sites at the gap of FeMo-co.In ammonia synthesis with iron catalysts,the N2-binding site might probably be the mode of 6Fe [μ6(η3,ε3)].
【关键词】 乙烯探针;
N2键合位;
固氮酶;
合成氨;
Fe催化剂;
【Key words】 Ethylene probe; N2-binding site; Nitrogenase; Ammonia synthesis; Iron catalysts;
【Key words】 Ethylene probe; N2-binding site; Nitrogenase; Ammonia synthesis; Iron catalysts;
【基金】 国家基础性研究重大关键项目
- 【文献出处】 高等学校化学学报 ,CHEMICAL RESEARCH IN CHINESE UNIVERSITIES , 编辑部邮箱 ,1995年06期
- 【分类号】O643.36
- 【被引频次】6
- 【下载频次】165