X-ray spectroscopic observation of an interstitial carbide in NifEN-bound FeMoco precursor.

X-ray spectroscopic observation of an interstitial carbide in NifEN-bound FeMoco precursor.
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DOI:
10.1021/ja309254g
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发表时间:
2013-01-16
影响因子:
15
通讯作者:
DeBeer, Serena
DeBeer, Serena
中科院分区:
化学1区
文献类型:
--
作者:
Lancaster, Kyle M.;Hu, Yilin;Bergmann, Uwe;Ribbe, Markus W.;DeBeer, Serena

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固氮酶的铁钼辅因子 (FeMoco) 含有生物学上前所未有的 μ6 配位 C4− 离子。尽管这种间隙原子在固氮酶催化中的作用尚不清楚,但在了解其生物合成起源方面已取得进展。在这里,我们报告了价核 (V2C) Fe Kβ X 射线发射光谱 (XES),以表明该 C4− 离子存在于 Fe8S9“L 簇”中,它是在插入钼和通过高柠檬酸盐配位之前 FeMoco 的直接前体。这些结果与支持 S-腺苷甲硫氨酸 (SAM) 依赖性酶 NifB 在将碳掺入固氮酶 FeMoco 中心中的作用的最新证据一致。
The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented μ6-coordinated C4− ion. Although the role of this interstitial atom in nitrogenase catalysis is unknown, progress has been made on understanding its biosynthetic origins. Here, we report valence-to-core (V2C) Fe Kβ X-ray emission spectroscopy (XES) to show that this C4− ion is present in the Fe8S9 “L-cluster,” which is the immediate precursor to FeMoco prior to the insertion of molybdenum and coordination by homocitrate. These results accord with recent evidence supporting a role for the S-adenosylmethionine (SAM)-dependent enzyme NifB in the incorporation of carbon into the FeMoco center of nitrogenase.
DOI: 10.1126/science.1224603
发表时间: 2012-09-28
期刊: Science (New York, N.Y.)
影响因子: --
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