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Synthesis and crystal structure of sodium ammonium dimeric (citrato)dioxovanadium(V) Na_2(NH_4)_4[VO_2(cit)]_2 centre dot 6H_2O

机译:钠二聚(柠檬酸)二氧钒钠(V)Na_2(NH_4)_4 [VO_2(cit)] _ 2中心点6H_2O的合成及晶体结构

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Recent crystallographic analysis of the metal centers in the nitrogenase molybdenum-iron protein with 0.22 and 0.27 nm resolution revealed the structural model of FeMo-cofactor as a cage-like cluster, in which molybdenum is chelated by hydroxy- and carboxylate ligands of homocitrate. It is deduced that the homocitrate may be important for the substrate reduction mechanism. Considering that the central molybdenum of nitrogenase can be replaced by vanadium, for better understanding the importance of homocitrate to the substrate mechanism, here the authors report the synthesis, spectra and crystal structure of a dimeric (citrato)oxovanadium(V) complex, in which vanadium is coordinated bidentately by the oxygen atoms of hydroxy- and carboxylate ligand in citrate anion.
机译:最近对0.22和0.27 nm分辨率的固氮酶钼铁蛋白中金属中心的晶体学分析显示,FeMo辅因子为笼状簇的结构模型,其中钼被纯柠檬酸盐的羟基和羧酸盐配体螯合。可以推断,均柠檬酸盐对于底物还原机理可能是重要的。考虑到氮酶的中心钼可以被钒代替,为了更好地理解均柠檬酸盐对底物机理的重要性,在此作者报告了二聚(柠檬酸)氧钒(V)配合物的合成,光谱和晶体结构,其中钒由柠檬酸根阴离子中的羟基和羧酸根配体的氧原子进行二齿配位。

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