靠近性联体调节细菌L. monocytogenes coproheme ferrochelatase中的活性部位结构和反应性
Andrea Dali1, Federico Sebastiani1, Thomas Gabler2
1Dipartimento di Chimica "Ugo Schiff" (DICUS), Università di Firenze, Via della Lastruccia 3-13, I-50019 Sesto Fiorentino (FI), Italy.
概括
铁酸酶将铁插入氨酸中进行血红素b生物合成. 用改变了His,Met或Phe的酶活性取代近端Tyr残留物,显示出弱铁协调是基质结合和产品释放的关键.
科学领域:
- 生物化学 生物化学
- 酶学 是一种酶学.
- 分子生物学分子生物学
背景情况:
- 铁糖酶是heme b生物合成中的关键酶,对于 prokaryotes 和 eukaryotes 都是必不可少的.
- 协调铁甲酸中铁甲酸的近位配体没有保存,其催化作用仍然不清楚.
研究的目的:
- 为了研究近位连接体在L. monocytogenes coproporphyrin ferrochelatase活性中的作用.
- 为了比较本地酶与Tyr被替换为His,Met或Phe的变体.
主要方法:
- 紫外线对电子吸收和共振拉曼光谱仪.
- 生物化学表征. 生物化学表征.
- 经典分子动力学 (MD) 模拟.
主要成果:
- 突变改变了基于近接联体极性的键相互作用和酶活性.
- 研究了Fe (III),Fe (II) 和Fe (II) -CO添加物形式.
- 通过近位残留物对氨酸铁的协调较弱或不存在被证实是必不可少的.
结论:
- 靠近的连接体的身份显著影响铁甲基酶的功能.
- 靠近位残留物对铁的弱协调对于基质结合和产品释放在血红素生物合成中至关重要.
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