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钼在固氮酶中氧化态和配位结构的研究

The study of the oxidation states and the coordination structure of Mo in N2 ase

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【作者】 倪新伯; 徐金龙; 汪勇先; 李粹芳; 许仁邦; 顾俭本; 沈巩懋;

【Author】 Ni Xinbo Xu Jinlong Wang Yongxian (Shanghai Institute of Nuclear Research, Academia Sinica)Li Cuifang Xu Renbang Gu Jianben Shen Gongmao (Shanghai In stit ute of Plant Physiology, Academia Sinica)

【机构】 中国科学院上海原子核研究所; 中国科学院上海植物生理研究所; 中国科学院上海植物生理研究所;

【摘要】 <正> 固氮酶是由Mo-Fe蛋白和Fe蛋白组成的。在Mo-Fe蛋白中含有二个Mo原子。在固氮酶的固氮反应机制中,Mo原子是络合底物、催化底物还原的活性中心原子。故研究Mo在Mo-Fe蛋白中的可能结构显得十分重要。

【Abstract】 N2ase is made up of two distinct and separately isolated proteins. An Fe protein and an Mo-Fe protein that has two Mo atoms per mole. 99Mo decays to excited nuclear state of 99Tc. The angular correlation of the 741-181keV γ rays were emitted subsequently in the deexcitation of the 99Tc through the medial state 5/2 + . 99Mo was incorporated in N2ase by jncubation. After freezing the solution of 99Mo labelled N2ase the attenuation factor G2 of PAC and quadrapole frequency ωe were determind. Compared with the G2 and ωe of other 99Mo labelled complexes, the oxidation state and coordination structure of 99Mo in N2ase were speculated. The mechanism of nitrogen fixation by N2ase was also discussed according to the principle of electron transformation.

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