部分氧化的铁钼蛋白的圆二色散谱和电子顺磁共振谱的研究  

STUDIES ON THE CIRCULAR DICHROISM (CD) AND ELECTRON PARAMAGNETIC RESONANCE (EPR)SPECTROSCOPY OF THE PARTIALLY OXIDIZED FeMo PROTEIN FROM AZOTOBACTER VINELANDII NITROGENASE

作　　者：黄巨富[1] 梅.查.麦肯纳 菲.杰.史蒂芬斯 

机构地区：[1]中国科学院植物研究所 [2]美国南加州大学化学系

出　　处：《Acta Botanica Sinica》1988年第1期46-53,共8页Acta Botanica Sinica（植物学报：英文版）

摘　　要：棕色固氮菌固氮酶 FeMo 蛋白与过量(5-6个当量)的酸性靛蓝保温30—60分钟后,蛋白中的 P-金属原子簇全部氧化,然而蛋白中的 FeMoCo 全都处于还原状态。Na_2S_2O_4使这种部分氧化的 FeMo 蛋白中的 P-cluster 重新还原,甲基紫精可加快这种还原。而亚甲蓝等氧化剂则使这种蛋白中的 FeMoCo 受到氧化。对这种部分氧化的 FeM。蛋白分别进行 CD 还原滴定和测定氧化过程中 EPR/ABS 的变化已经得到 P-cluster 和 FeMoCo 的氧化还原当量数目。After nitrogenase FeMo protein from A.vinelandii was incubated with a large excess (5—6 equivalents) of indigo carmine for 30—60 min.,all of P-clusters in the partially oxidized FeMo protein were oxidized,but all of FeMoCo in the protein were still in the reductive state.The oxidized P-clusters in the protein were able to be completely reduced by Na_2S_2O_4(DT)and the reduction was accelerated by methyl viologen (MV).And all of FeMoCo in the protein were firstly oxidized by some oxidants such as methylene blue.The numbers of the redox equiva- lent of P-cluster and FeMoCo have been obtained by the CD reductive titration of and EPR/ ABS time course on the oxidation of the partially oxidized FeMo protein,respectivelly.

关 键 词：部分氧化 铁钼蛋白 圆二色散谱 电子顺磁共振谱 酸性靛蓝 氧化还原 棕色固氮菌 固氮酶 

分 类 号：Q936[生物学—微生物学]