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1.中国科学院上海原子核研究所
2.中国科学院上海植物生理研究所
收稿日期:1984-08-04,
纸质出版日期:1985-12
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倪新伯, 徐金龙, 汪勇先, 等. 钼在固氮酶中氧化态和配位结构的研究[J]. 核技术, 1985,08(9):18-20,52.
Xinbo Ni, Jinlong Xu, Yongxian Wang, et al. The study of the oxidation states and the coordination structure of Mo in N2 ase[J]. Nuclear techniques, 1985, 08(9): 18-20,52.
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
[1]
。故研究Mo在Mo-Fe蛋白中的可能结构显得十分重要。
N
2
ase 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.
99
Mo decays to excited nuclear state of
99
Tc. The angular correlation of the 741—181keV γ rays were emitted subsequently in the deexcitation of the
99
Tc through the medial state 5/2 +.
99
Mo was incorporated in N
2
ase by incubation. After freezing the solution of
99
Mo labelled N
2
ase the attenuation factor G
2
of PAC and quadrapole frequency
ω
e were determind. Compared with the G
2
and
ω
e of other
99
Mo labelled complexes
the oxidation state and coordination structure of
99
Mo in N
2
ase were speculated. The mechanism of nitrogen fixation by N
2
ase was also discussed according to the principle of electron transformation.
B. E. Smith , J . Less Common Metals , 54 , 465 ( 1977 ).
R. M. Steffen , Phys. Rev ., 103 , 116 ( 1956 ).
P. DA. R. Andrade et al ., Nuclear physics , 66 , 545 ( 1965 ).
李粹芳 等 , 植物生理学报 , 10 , 1 , 47 ( 1984 ).
扰动角关联组 , 核技术 , 1 , 32 ( 1979 ).
J. R. Knox et al ., Chem. Commun ., 1227 ( 1968 ).
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