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首页> 外文期刊>Journal of Molecular Biology >A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase
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A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase

机译：一个对人铁螯合酶中的卟啉去质子化和产物释放有选择性的π-螺旋开关

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Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Due to the many critical roles of heme, synthesis of heme is required by the vast majority of organisms. Despite significant investigation of both the microbial and eukaryotic enzyme, details of metal chelation remain unidentified. Here we present the first structure of the wild-type human enzyme, a lead-inhibited intermediate of the wild-type enzyme with bound metallated porphyrin macrocycle, the product bound form of the enzyme, and a higher resolution model for the substrate-bound form of the E343K variant. These data paint a picture of an enzyme that undergoes significant changes in secondary structure during the catalytic cycle. The role that these structural alterations play in overall catalysis and potential protein-protein interactions with other proteins, as well as the possible molecular basis for these changes, is discussed. The atomic details and structural rearrangements presented herein significantly advance our understanding of the substrate binding mode of ferrochelatase and reveal new conformational changes in a structurally conserved pi-helix that is predicted to have a central role in product release. (C) 2007 Elsevier Ltd. All rights reserved.
机译：铁螯合酶（原血红素铁酶，EC 4.99.1.1）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（血红素）。由于血红素的许多关键作用，绝大多数生物都需要合成血红素。尽管对微生物和真核生物酶都进行了大量研究，但金属螯合的细节仍不清楚。在这里，我们介绍了野生型人类酶的第一个结构，具有结合的金属化卟啉大环的野生型酶的铅抑制中间体，酶的产物结合形式以及底物结合形式的高分辨率模型E343K变体的这些数据描绘了酶在催化循环中二级结构发生重大变化的情况。讨论了这些结构改变在整体催化中的作用以及与其他蛋白质的潜在蛋白质-蛋白质相互作用，以及这些改变的可能分子基础。本文介绍的原子细节和结构重排显着提高了我们对亚铁螯合酶底物结合模式的理解，并揭示了结构保守的pi-螺旋中新的构象变化，预计其在产物释放中起关键作用。 （C）2007 Elsevier Ltd.保留所有权利。

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