(Peer-Reviewed) Radical SAM-Dependent Demetallation of Heme
Jinduo Cheng 程金铎 ¹, Wei Ding 丁伟 ², Qi Zhang 张琪 ¹
¹ Department of Chemistry, Fudan University, Shanghai, 200433 China
中国 上海 复旦大学化学系
² State Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240 China
中国 上海 上海交通大学生命科学技术学院 微生物代谢国家重点实验室
Abstract
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.
Integrated metasurface-freeform system enabled multi-focal planes augmented reality display
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Opto-Electronic Science
2026-01-23
