首页> 美国卫生研究院文献>Biochemical Journal >Iron K-edge X-ray-absorption spectroscopy of the iron-vanadium cofactor of the vanadium nitrogenase from Azotobacter chroococcum.
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Iron K-edge X-ray-absorption spectroscopy of the iron-vanadium cofactor of the vanadium nitrogenase from Azotobacter chroococcum.

机译:嗜铬固氮菌中钒固氮酶的铁-钒辅因子的铁K边缘X射线吸收光谱。

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摘要

Iron K-edge e.x.a.f.s. data for the iron-vanadium cofactor (FeVaco) from Azotobacter chroococcum vanadium nitrogenase reported here provide further evidence for the structural similarity between this and the iron-molybdenum nitrogenase cofactor (FeMoco) from Klebsiella pneumoniae molybdenum nitrogenase [Arber, Flood, Garner, Gormal, Hasnain & Smith (1988) Biochem. J. 252, 421-425]. The e.x.a.f.s. data are consistent with the vanadium being present in a V-Fe-S cluster, thus confirming that the N-methylformamide extract of the VFe protein component of A. chroococcum vanadium nitrogenase does indeed contain a polynuclear metal-sulphur cluster. Additionally, a long Fe-Fe distance is observed as 0.369 nm, demonstrating the presence of a long-range order in the cluster.
机译:铁K边缘e.x.a.f.s.此处报道的绿脓杆菌钒氮酶的铁-钒辅酶(FeVaco)数据提供了进一步的证据,证明其与肺炎克雷伯菌钼-氮酶的铁-钼固氮酶辅因子(FeMoco)之间存在结构相似性[Arber,Flood,Garner,Gormal, Hasnain&Smith(1988)生物化学。 J. 252,421-425]。 e.x.a.f.s.数据与V-Fe-S簇中存在的钒一致,因此证实了嗜铬球菌钒氮酶的VFe蛋白组分的N-甲基甲酰胺提取物确实含有多核金属-硫簇。此外,观察到长的Fe-Fe距离为0.369 nm,这表明簇中存在长程有序。

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