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dc.contributor.advisor周朝晖
dc.contributor.author张荣华
dc.date.accessioned2016-02-14T03:08:18Z
dc.date.available2016-02-14T03:08:18Z
dc.date.issued2009-12-08 16:03:48.0
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/34576
dc.description.abstract固氮酶是某些微生物在常温常压下固氮成氨的催化剂,其催化作用机理和化学模拟一直是国际上长期致力研究的对象。钼铁蛋白的单晶高分辨X光衍射分析表明,固氮酶催化活性中心铁钼辅基的结构为MoFe7S9X(homocit)(X=C,NorO)。其中,Mo原子处于一端的角落位置上,并和3个3-硫配体、一个组氨酸和一个高柠檬酸配位,形成八面体的络合物。高柠檬酸以-烷氧基氧和-羧基氧与钼形成双齿配位。研究表明,含有高柠檬酸的固氮酶的固氮活性比其它羟基羧酸突变种的固氮酶活性强,但是什么原因造成的这种差别目前还没有定论。此外,最新研究表明,在固氮酶铁钼辅基的生物合成过...
dc.description.abstractNitrogenase catalyzes the reduction of dinitrogen to ammonia in the process of biological nitrogen fixation. In the past few decades, its catalytic mechanism and chemical simulation have been widely studied. The high resolution (1.16 Å) X-ray structural analysis of the MoFe protein of nitrogenase reveals the iron molybdenum cofactor (FeMo-co) as a cage structure, MoFe7S9X(homocit) (X = C, N ...
dc.language.isozh_CN
dc.relation.urihttps://catalog.xmu.edu.cn/opac/openlink.php?strText=22755&doctype=ALL&strSearchType=callno
dc.source.urihttps://etd.xmu.edu.cn/detail.asp?serial=23648
dc.subject
dc.subject
dc.subject羟基羧酸
dc.subject铁钼辅基
dc.subjectmolybdenum
dc.subjecttungsten
dc.subjecthydroxycarboxylic acids
dc.subjectFeMo-co
dc.title柠檬酸、苹果酸和柠苹酸钼(钨)配合物研究
dc.title.alternativeStudies on molybdenum and tungsten complexes with citrate, malate and citramalate
dc.typethesis
dc.date.replied2009-06-11
dc.description.note学位:理学博士
dc.description.note院系专业:化学化工学院化学系_物理化学(含化学物理)
dc.description.note学号:20520060153266


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