通过NRVS和DFT揭示的黄铁NO还原酶的氧桥活性位点
Filipe Folgosa1, Vladimir Pelmenschikov2, Giorgio Caserta2
1Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras 2780-157, Portugal.
概括
黄铁蛋白 (FDPs) 使用二铁活性位点来排毒反应性中间体. 我们使用57Fe NRVS揭示了FDP活性部位的氧化还原相关结构变化,澄清了其协调环境和反应性.
科学领域:
- 生物化学和分子生物学
- 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:
- 生物利用氧气和酸盐作为能量来源,需要对反应性中间体进行排毒.
- 黄铁蛋白 (FDPs) 对于NO和O2排毒至关重要,它采用了二铁活性部位.
- 由于数据相互矛盾,FDP二氧化活性站点的精确协调环境受到争议.
研究的目的:
- 为了阐明来自大肠杆菌的黄铁蛋白 (FDP) 的氧化还原相关结构变化.
- 为了确定FDP中的二铁活性位点的确切协调环境.
- 为了解二氧化铁酶中的氧化还原连接连接体动力学提供一种机制框架.
主要方法:
- 使用了57Fe核共振振动光谱仪 (NRVS).
- 补充了NRVS与Mössbauer光谱和密度函数理论 (DFT) 的计算.
- 在减少后对FDP活跃地点的结构变化进行了调查.
主要成果:
- 作为隔离的差异性状态具有二氧桥梁Fe (III) - - - - - - - - - - - - - - - - - - - - - - - - Fe (III) 核心.
- 通过减少,通过失去桥接联体,导致一个单氧Fe (II) - (μOH-) -Fe (II) 中心.
- 在NRVS条件下,光减光可以发生,可能会诱导微妙的氧化还原变化.
结论:
- 干重组定义了FDPs中氧化还原连接活性的结构基础.
- 这些发现为解释二铁酶中的氧化还原连接联体动态提供了机制框架.
- 结果对其他含有二活性位点的酶类有广泛的影响.
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