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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Substrate interactions with human ferrochelatase
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Substrate interactions with human ferrochelatase

机译：底物与人铁螯合酶的相互作用

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摘要

Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Human ferrochelatase is a homodimeric, inner mitochondrial membrane-associated enzyme that possesses an essential [2Fe-2S] cluster. In this work, we report the crystal structure of human ferrochelatase with the substrate protoporphyrin IX bound as well as a higher resolution structure of the R115L variant without bound substrate. The data presented reveal that the porphyrin substrate is bound deep within an enclosed pocket. When compared with the location of N-methylmesopor-phyrin in the Bacillus subtilis ferrochelatase, the porphyrin is rotated by by ≈100° and is buried an additional 4.5 A deeper within the active site. The propionate groups of the substrate do not protrude into solvent and are bound in a manner similar to what has been observed in uroporphyrinogen decarboxylase. Furthermore, in the substrate-bound form, the jaws of the active site mouth are closed so that the porphyrin substrate is completely engulfed in the pocket. These data provide insights that will aid in the determination of the mechanism for ferrochelatase.
机译：铁螯合酶是血红素生物合成中的末端酶，催化亚铁插入原卟啉IX中形成原血红素IX。人铁螯合酶是同型二聚体，内部线粒体膜相关酶，具有必需的[2Fe-2S]簇。在这项工作中，我们报告了人类铁螯合酶的晶体结构与底物原卟啉IX结合以及没有结合底物的R115L变体的更高分辨率结构。呈现的数据表明，卟啉底物在封闭的口袋内深处结合。与枯草芽孢杆菌铁螯合酶中的N-甲基中磷-卟啉位置相比，卟啉旋转≈100°，并在活性位点内深埋4.5A。底物的丙酸酯基团不突出到溶剂中并且以与在尿卟啉原原脱羧酶中观察到的相似的方式结合。此外，在与基质结合的形式中，活动部位口的颚闭合，从而使卟啉基质完全被袋囊吞没。这些数据提供了有助于确定铁螯合酶机制的见解。

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