从固氮酶中分离出钼铁簇。
Isolation of a molybdenum--iron cluster from nitrogenase.
作者信息
Shah V K, Brill W J
出版信息
Proc Natl Acad Sci U S A. 1981 Jun;78(6):3438-40. doi: 10.1073/pnas.78.6.3438.
Abstract
A molybdenum-iron cluster (Mo-Fe cluster) containing 6 Fe atoms per Mo was isolated by methyl ethyl ketone extraction of component I of nitrogenase from Azotobacter vinelandii. The cluster has no EPR signal in the g = 4 region but has an intense signal at g = 2.05 and 2.01. After the cluster was transferred from methyl ethyl ketone to N-methylformamide, the signal in the g = 2 region disappeared and a signal similar to that found with Fe-Mo cofactor appeared. The Mo-Fe cluster is the EPR-active center that undergoes reversible oxidation-reduction during catalytic turnover at the active site of the enzyme. In contrast to the Fe-Mo cofactor, which contains 8 Fe atoms per Mo, the Mo-Fe cluster failed to activate either inactive component I in extracts of A. vinelandii mutant strain UW45 or tungsten-containing component I from wild-type A. vinelandii. On the other hand, the Mo-Fe cluster showed as much acetylene-reduction activity with sodium borohydride as the reductant as did the Fe-Mo cofactor. Like nitrogenase-dependent and Fe-Mo cofactor-dependent acetylene reduction, the Mo-Fe cluster-dependent acetylene reduction is strongly inhibited by carbon monoxide.
摘要
通过用甲乙酮萃取来自棕色固氮菌的固氮酶组分I，分离出了每个钼含有6个铁原子的钼铁簇（Mo-Fe簇）。该簇在g = 4区域没有电子顺磁共振（EPR）信号，但在g = 2.05和2.01处有强信号。当该簇从甲乙酮转移到N-甲基甲酰胺后，g = 2区域的信号消失，出现了一个与铁钼辅因子相似的信号。Mo-Fe簇是在酶的活性位点催化周转过程中经历可逆氧化还原的EPR活性中心。与每个钼含有8个铁原子的铁钼辅因子不同，Mo-Fe簇不能激活棕色固氮菌突变株UW45提取物中的无活性组分I或来自野生型棕色固氮菌的含钨组分I。另一方面，Mo-Fe簇与铁钼辅因子一样，以硼氢化钠作为还原剂时表现出同样多的乙炔还原活性。与依赖固氮酶和依赖铁钼辅因子的乙炔还原一样，依赖Mo-Fe簇的乙炔还原受到一氧化碳的强烈抑制。
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