Radical SAM-Dependent Demetallation of Heme
作者机构：Department of ChemistryFudan UniversityShanghai 200433China State Key Laboratory of Microbial MetabolismSchool of Life Sciences&BiotechnologyShanghai Jiao Tong UniversityShanghai 200240China
出 版 物：《Chinese Journal of Chemistry》 (中国化学（英文版）)
年 卷 期：2022年第40卷第9期
页 面：1053-1058页
核心收录：
学科分类：07[理学] 070303[理学-有机化学] 0703[理学-化学]
基 金：This work is supported by grants from the National Key Researchand Development Program(2021YFA0910501 and 2018YFA0900402) the National Natural Science Foundation of China(21822703,21921003,and 32070050) the funding of Innovative Research Team of High-level Local Universities in Shanghai and a key laboratory program of the Education Commission of Shanghai Municipality(ZDSYS14005).
主 题：Biosynthesis Biotransformations Cofactors Enzymes Hemin
摘 要：Demetallation of heme to release iron is a chemical difficult reaction and is highly rare in biochemistry,with apoferritin as the only known enzyme responsible for this process.Here we show the heme degradation enzyme Chuw catalyzes heme demetallation besides its known methyltransferase activity(which converts heme to a ring-open product anaerobilin).We show the demetallation activity of Chuw is radical SAM-dependent,and likely involves the same set of intermediates involved in the anaerobilin-producing pathway.The ChuW-catalyzed demetallation reaction does not require external reductant,and can occur on several heme analogs with different metal centers.These findings establish a brand-new chemistry in the radical SAM enzymes,highlighting the remarkable catalytic diversity of this superfamily of enzymes.
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