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钼,铁,硫化合物激活曝氧的棕色固氮菌固氮酶钼铁蛋白的研究
引用本文:黄巨富 王熬金. 钼,铁,硫化合物激活曝氧的棕色固氮菌固氮酶钼铁蛋白的研究[J]. Acta Botanica Sinica, 1989, 31(10): 785-791
作者姓名:黄巨富 王熬金
作者单位:中国科学院植物研究所 北京100044(黄巨富,骆爱玲,解雪梅),中国科学院生物物理研究所 北京100080(王熬金)
基金项目:中国科学院科学基金,国家自然科学基金资助的课题
摘    要:曝氧后,棕色固氮菌(Azotobacter vinelandii)固氮酶钼铁蛋白的催化活性和圆二色信号都显著降低,而吸收光谱则显著增加。与钼、铁、硫化合物和二硫苏糖醇组成的重组溶液保温后,曝氢蛋白的圆二色信号和吸收光谱几乎完全恢复至天然状态的同时,乙炔还原活性也得到了显著的恢复,表明重组溶液可使曝氧蛋白中的 P-cluster和其它活性部位都得到了不同程度的修复。

关 键 词:圆二色谱  蛋白激活  曝氧钼铁蛋白  棕色固氮菌固氮酶

STUDIES ON THE REACTIVATION OF AERATED NITROGENASE MoFe PROTEIN FROM AZOTOBACTER VINELANDII BY THE COMPOUNDS OF IRON MOLYBDENUM AND SULFUR
Huang Ju-fu Luo Ai-ling Xie Xue-mei. STUDIES ON THE REACTIVATION OF AERATED NITROGENASE MoFe PROTEIN FROM AZOTOBACTER VINELANDII BY THE COMPOUNDS OF IRON MOLYBDENUM AND SULFUR[J]. , 1989, 31(10): 785-791
Authors:Huang Ju-fu Luo Ai-ling Xie Xue-mei
Abstract:After the exposure to air,the crystalline nitrogenase MoFe protein from Azotobacter vine- dii was resulted in the remarkable increase in its absorption (ABS) and the significant decrease in its activity and circular dichroism(CD) However,when the aerated MoFe pro- ein was incubated with the reconstituting solution which consisted of Na_2MoO_4,ferric citra- te,Na_2S aud dithiothreitol,the ABS and CD of the aerated MoFe protein both were comple- tely restored,simultaneously with the significant restoration of acetylene reduction.It is shown that the P-cluster and other parts related to the protein activity which was damaged by O_2 are able to be repaired to a certain extent by the reconstituting solution.
Keywords:Circular dichroism spectrum  Protein reconstitution  Aerated MoFe protein  Nitrogenase from Azotobacter vinelandit  
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