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在细菌硫酸盐氧化酶中对pH依赖的Mo (V) 物种进行结构和光谱研究

Ahmed Djeghader¹, Julia Rendon², Frédéric Biaso²

¹Department of Chemical Sciences and Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.

Inorganic chemistry

|November 19, 2024

概括

硫酸盐氧化酶 (SOE) 通过将硫酸盐转化为硫酸盐来保护细胞. 这项研究揭示了酸盐结合如何稳定活性部位,并揭示了各种生物体中保存的催化机制.

科学领域:

生物化学生化学
酶学是一种酶学.
结构生物学结构生物学

背景情况:

硫酸盐氧化酶 (SOE) 是所有生命形式中发现的含有的重要酶.
它们催化了硫酸盐的氧化到硫酸盐,这对于保护细胞免受硫酸盐毒性的作用至关重要.
之前的研究已经确定了*Thermus thermophilus*硫酸盐脱酶 (TtSDH) 中的原子与原子的酸盐协调.

研究的目的:

阐明在TtSDH中酸盐 adduct 稳定性的结构和机制基础.
用电子磁共振 (EPR) 光谱来研究酶活性位点的pH依赖性行为.
来自不同生物体的SOE的保存活性站点属性的特征.

主要方法:

进行X射线晶体学以确定未结合的酶结构.
电子磁共振 (EPR) 光谱在广泛的pH范围.
HYSCORE,H2O/D2O交换,以及密度函数理论 (DFT) 的计算.

主要成果:

不结合的TtSDH结构揭示了环境的结网的变化.
这些变化稳定了先前观察到的酸盐添加物.
EPR研究发现了pH依赖的Mo(V) 物种,这是真核生物SOE的特征.
在细菌SOE中实现了以前未报告的低pHMo(V) 物种的详细表征.

结论:

结网对于稳定活性部位的添加物至关重要.
细菌和真核SOE共享保存的活性位点特性,包括pH依赖的MoV物种.
这突显了SOE机制在各种生命形式的进化保护.

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