多核铁物种的蛋白质模板驱动的形成
Simon A Malone1, Allison Lewin, Mehmet A Kilic
1School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, UK.
Journal of the American Chemical Society
|January 15, 2004
概括
突变的费里丁不能形成24-基结构,仍然会结合和氧化铁,形成. 这表明细菌铁素内有特定的核化部位用于铁核形成.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 蛋白质化学 蛋白质化学
背景情况:
- 费里丁是铁储存蛋白质,具有24个多外,可储存多达4500个Fe3+) 离子.
- 大肠杆菌和Rhodobacter capsulatus细菌的突变阻止了24-meric组装,稳定了二分体形式.
研究的目的:
- 为了研究铁结合和集群形成的细菌酸二聚体.
- 探索蛋白质结构在铁核和储存中的作用.
主要方法:
- 局部定向的突变发生产生Glu128Arg/Glu135Arg突变物.
- 在蛋白质二次体中添加Fe(2+) 的有氧添加.
- 凝透色谱和沉积平衡研究.
- 电子偏磁共振 (EPR) 光谱学.电子偏磁共振 (EPR) 光谱学.
- 铁化试验. 铁化试验.
主要成果:
- 突变二极体结合并氧化Fe(2+) 到Fe(3+),形成反铁磁合的铁团.
- 铁离子仍然与二极体相关,由染色学和沉积表示.
- 通过化剂缓慢去除铁表明特定的结合点,而不是偶然的关联.
- EPR信号证实了二度体内铁集群的形成.
结论:
- 细菌酸二聚体具有矿物核形成的核化部位.
- 铁储存在细菌酸盐中涉及蛋白质介导核化,而不仅仅是被动水解.
- 结构分析和序列比较表明潜在的铁核化地点.
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