来自Synechocystis sp. 的 [4Fe4S] 铁素类蛋白质的结构和生物物理特性. PCC 6803具有独特的两个域结构
Effie Kisgeropoulos1, Vivek S Bharadwaj2, Anastasia Ledinina3
1Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, USA.
Journal of inorganic biochemistry
|November 26, 2023
概括
这项研究揭示了Ferredoxin 9,Synechocystis中独特的电子载体蛋白质,协调多个铁硫. 它的独特结构和特性表明它在蓝藻细菌和其他生物中保留了作用.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 电子载体蛋白 (ECP) 对于代谢和光合作用途径至关重要,促进电子转移.
- 综合囊 sp. 的情况. PCC 6803具有至少九种铁毒素 (Fdxs) 的复杂网络,之前的研究提供了有限的功能洞察力.
- 铁素9 (Fdx9) 是一种新的ECP,与正规铁素相比,它具有独特的结构和电子特征.
研究的目的:
- 研究来自Synechocystis sp.的费雷多克辛9 (slr2059) 的结构和功能特性. 在PCC 6803中.
- 阐明铁硫集群的协调和Fdx9.9的氧化还原特性.
- 探索Fdx9.9的进化保护和潜在的功能平行.
主要方法:
- 序列分析和计算建模以确定Fdx9独特的两个域架构.
- 用于实验分析的Fdx9的异质生产.
- 电子偏磁共振 (EPR) 光谱和正方波电压测量以表征氧化还原活性集群和潜力.
主要成果:
- Fdx9表现出一种独特的双域结构,包括一个N端的Nil域和一个C端的铁硫结合域.
- Fdx9 坐标两个氧化还原活性 [4Fe4S] 集群,测量的氧化还原电位为 -420 ± 9 mV 和 -516 ± 10 mV 与 SHE 相比.
- 模型显示Fdx9的中性至基本蛋白质表面,与PetF等正规铁毒素的酸性表面形成鲜明对比.
结论:
- 铁素9是一种独特的多域铁素,协调多个 [4Fe4S] 集群,与典型的 [2Fe2S] 铁素不同.
- 尼尔-2[4Fe4S]多域铁素类型在蓝藻细菌中保存,这表明它具有显著的进化重要性.
- 结构上的相似性将Fdx9与参与甲基体内同型氨酸合成的蛋白质联系起来,暗示其功能性作用得到保护.
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