高等学校化学学报

高等学校化学学报 ›› 1995, Vol. 16 ›› Issue (6): 920.

• 论文 • 上一篇    下一篇

固氮酶及合成氨Fe催化剂中N2的络合位

黄静伟1, 张风章2, 许良树2, 张鸿图1, 万惠霖1, 蔡启瑞1   

  1. 1. 厦门大学化学系, 厦门, 361005;
    2. 厦门大学生物学系, 厦门, 361005
  • 收稿日期:1994-12-07 修回日期:1995-03-05 出版日期:1995-06-24 发布日期:1995-06-24
  • 通讯作者: 黄静伟,男,28岁,博士,讲师.
  • 作者简介:黄静伟,男,28岁,博士,讲师.
  • 基金资助:

    国家基础性研究重大关键项目

N2-Binding Site in Nitrogenase and Ammonia Synthesis with Iron Catalysts

HUANG Jin-Wei1, ZHANG Feng-Zhang2, XU Liang-Shu2, ZHUANG Hong-Tu1, WAN Hui-Lin1, CAI Qi-Rui1   

  1. 1. Department of Chemistry, Xiamen University, Xiamen, 361005;
    2. Department of Biology, Xiamen University, Xiamen, 361005
  • Received:1994-12-07 Revised:1995-03-05 Online:1995-06-24 Published:1995-06-24

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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).

关键词: 乙烯探针, N2键合位, 固氮酶, 合成氨, Fe催化剂

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,ε4)]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)].

Key words: Ethylene probe, N2-binding site, Nitrogenase, Ammonia synthesis, Iron catalysts

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