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固氮酶铁钼辅基在分离纯化中结构变化的新证据
引用本文:张凤章,黄河清,龙敏南,邱雪慧,许良树.固氮酶铁钼辅基在分离纯化中结构变化的新证据[J].中国生物化学与分子生物学报,1999,15(2):328-331.
作者姓名:张凤章  黄河清  龙敏南  邱雪慧  许良树
作者单位:厦门大学生物学系
摘    要:根据Kim-Rees模型[1],固氮酶铁钼辅基(即FeMoco或M簇),是由一个MoFe3S3簇和一个Fe4S3簇通过三个S-桥联接而成.然而,自Shah等(1977)首次从结晶的钼铁蛋白中分离出具有生物重组活性的FeMoco以来,固氮研究者们一直致...

收稿时间:1999-04-20

New Evidence for Structure Change of Iron molybdenum Cofactor from Nitrogenase MoFe Protein in Separation
ZHANG Fengzhang,HUAN Heqing,LONG Minnan,QIU Xuehui,XU Liangshu.New Evidence for Structure Change of Iron molybdenum Cofactor from Nitrogenase MoFe Protein in Separation[J].Chinese Journal of Biochemistry and Molecular Biology,1999,15(2):328-331.
Authors:ZHANG Fengzhang  HUAN Heqing  LONG Minnan  QIU Xuehui  XU Liangshu
Institution:(Department of Biology,Xiamen University,Xiamen 361005
Abstract:The iron molybdenum cofactor (FeMoco) of nitrogenase MoFe protein from Azotobacter Vinelandii OP was extracted by N methylformamide (NMF).Effects of FeMoco(in NMF) on electronic spectrum and fluorescence intensity (in 1 mol/L NaOH) were investigated by fluorophotometric titrations and compared with results of effects of (NH 4) 2MoS 4 and its complexes with Na 2S,Na 2S 2 and (NH 4) 2S X on relative properties of FDMA.It was found that titration curve for quenching of FDMA with FeMoco was very similar to that for quenching of FDMA with complexes of (NH 4) 2MoS 4 and Na 2S 2(1∶3,mol/mol).The results showed that FeMoco(N) probably contained S S bonds and Its structure was found to be a changing one.
Keywords:Nitrogenase  Iron  molybdenum cofactor  Fluorophotometric titration  Structural change  
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