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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural Consequences Of Effector Protein Complex Formation In A Diiron Hydroxylase
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Structural Consequences Of Effector Protein Complex Formation In A Diiron Hydroxylase

机译：Diiron羟化酶中效应蛋白复合物形成的结构后果。

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摘要

Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 A from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.
机译：羧酸桥联的二铁羟化酶是负责多种烃分解代谢的多组分酶复合物，因此因其作用机理以及在生物修复和酶促合成中的潜在用途而引起人们的关注。这些酶复合物使用小分子量效应蛋白来调节羟化酶的功能。但是，这些功能更改的起源了解甚少。在这里，我们报告的甲苯4-单加氧酶在2个氧化还原状态的生物学相关效应蛋白-羟化酶复合物的结构。该结构揭示了许多协调的变化，这些变化发生在从活性位起直至25 A的温度，并保持了二恶铁中心的催化作用。结果为观察到的与效应蛋白结合相关的许多可测量性质的变化提供了结构基础。该描述提供了对效应蛋白结合在所有羧酸酯桥联的二铁羟化酶中的功能性作用的见解。

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