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Dph3 通过捐赠一个铁原子来转化 Dph1-Dph2 中的 [3Fe-4S] 到 [4Fe-4S] 集群来实现有氧二甲胺生物合成

Yugang Zhang¹, Dan Su¹, Boris Dzikovski¹

¹Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.

Journal of the American Chemical Society

|June 22, 2021

概括

激进的S-adenosylmethionine酶需要铁硫集群才能发挥作用. 一种名为Dph3的蛋白质有助于在氧气的存在下维持这些,使酶在有氧环境中活动.

科学领域:

生物化学
酵素学
蛋白质的结构和功能

背景情况:

激进的S-adenosylmethionine (激进的SAM) 酶对于各种生物过程至关重要.
这些酶依赖于 [4Fe-4S] 的催化活性.
众所周知, [4Fe-4S] 集群对氧气非常敏感,对有氧生物的酶功能构成挑战.

研究的目的:

研究激素-SAM酶,特别是二胺生物合成酶Dph1-Dph2在氧气存在时如何保持活性.
阐明铁硫团在Dph1-Dph2酶复合体中的作用.
探索在有氧环境中保存激素-SAM酶功能的潜在机制.

主要方法:

研究了酵母Dph1-Dph2酶复合体.
在有氧条件下研究了 [4Fe-4S] 集群的稳定性和转变.
分析了Dph1-Dph2和铁捐赠蛋白Dph3之间的相互作用.

主要成果:

在 Dph1-Dph2 中的 [4Fe-4S] 集群在氧气的存在下容易降解为 [3Fe-4S] 集群.
发现小蛋白Dph3向 [3Fe-4S] 集群捐赠了一个铁原子.
这种铁捐赠将降解的集群转化为功能 [4Fe-4S] 集群,在其催化周期中恢复 Dph1-Dph2 活性.

结论:

一种涉及Dph3蛋白的新机制允许在有氧条件下在激素-SAM酶中维持功能 [4Fe-4S] 集群.
这种铁捐赠策略可能是保持其他激素-SAM酶在富含氧气环境中的一般机制.
Dph3类蛋白质的存在可能对有氧生物中的各种激素-SAM酶的功能至关重要.

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