铁矿化由细菌铁素的结构基础
Allister Crow1, Tamara L Lawson, Allison Lewin
1Centre for Molecular and Structural Biochemistry, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, UK.
Journal of the American Chemical Society
|April 28, 2009
概括
这项研究揭示了细菌 (BFR) 如何矿化铁,显示其铁氧化酶中心作为催化辅因子. 一个新的内部铁部位有助于电子转移,这表明BFR.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- 费里丁蛋白通过其核心内的矿化来管理细胞铁.
- 细菌铁素 (BFR) 是一种具有独特铁矿化机制的细菌铁素.
- 了解BFR的机制,可以了解铁的稳态和进化.
研究的目的:
- 为了阐明在细菌铁中铁矿化机制 (BFR).
- 描述铁氧化酶中心和BFR中的新铁结合点的作用.
- 为了比较BFR的机制与真核生物蛋白和相关蛋白质.
主要方法:
- 进行X射线晶体学以确定BFR结构 (apo,di-Fe(2+),di-Fe(3+)).
- 野生类型和突变BFR变体的动力学研究.
- 对铁结合点和电子转移通路的分析.
主要成果:
- BFR铁氧化酶中心是为Fe2+结合和氧化预制的.
- 形成了一个稳定的mu-oxo桥梁di-Fe(3+) 中心,没有直接转移到核心.
- 一个新的内部表面Fe(2+) 位点 (His46,Asp50) 被确定并得到了功能验证.
- 铁氧化酶中心具有催化作用,与真核生物酸孔模型不同.
- 内部表面的位置促进了Fe2+) 氧化过程中的电子转移.
结论:
- 细菌瑞丁利用催化铁氧化酶中心进行铁矿化.
- 一个新的内部铁位点对于BFR中的电子转移至关重要.
- BFR的机制可能代表了与其他二铁蛋白的进化联系.
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