酶FeMo辅因子的间位原子:ENDOR和ESEEM证据表明它不是一个
Tran-Chin Yang1, Nathan K Maeser, Mikhail Laryukhin
1Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA.
Journal of the American Chemical Society
|September 15, 2005
概括
这种酶MoFe蛋白质的化酶.
科学领域:
- 生物化学 生物化学
- 生物有机化学 生物有机化学
- 结构生物学 结构生物学
背景情况:
- 化酶复合体对于生物固定的作用至关重要.
- MoFe蛋白的活性部位含有复杂的[MoFe7S9:同酸盐]FeMo辅因子.
- 之前的X射线结晶学表明FeMo辅因子内有一个未知的原子 (X).
研究的目的:
- 为了确定FeMo辅因子中的未识别的原子 (X) 是否是.
- 为了研究酶MoFe蛋白的活性位点的组成.
主要方法:
- 使用X射线晶体学来确定X原子的电子密度.
- 采用了Q频段电子核双共振 (ENDOR) 和电子自旋回声封膜调制 (ESEEM) 光谱仪.
- 来自MoFe蛋白和用14N或15N同位素培养的NMF提取的FeMo辅因子的光谱信号的比较.
主要成果:
- 观察到与单个N,O或C原子一致的电子密度.
- 归因于 (14N或15N) 的光谱信号仅与蛋白质有关.
- 这些特异性信号在提取FeMo辅因子时丢失.
结论:
- 在FeMo辅因子中的未识别的X原子不是.
- 通过光谱检测到的原子位于蛋白质成分中,而不是FeMo辅因子本身.
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