Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis
Conventional heme enzymes utilize iron–oxygen intermediates to activate substrates and drive reactions. Recently, Chen et al. discovered a novel NADPH-independent superoxide mechanism of heme catalase EasC, which facilitates an O2-dependent radical oxidative cyclization reaction during ergot alkaloi...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-06-01
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| Series: | Engineering Microbiology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667370325000219 |
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| author | Yuanyuan Jiang Zhong Li Shengying Li |
| author_facet | Yuanyuan Jiang Zhong Li Shengying Li |
| author_sort | Yuanyuan Jiang |
| collection | DOAJ |
| description | Conventional heme enzymes utilize iron–oxygen intermediates to activate substrates and drive reactions. Recently, Chen et al. discovered a novel NADPH-independent superoxide mechanism of heme catalase EasC, which facilitates an O2-dependent radical oxidative cyclization reaction during ergot alkaloid biosynthesis. This enzyme coordinates superoxide-mediated catalysis by connecting spatially distinct NADPH-binding pocket and heme pocket via a slender tunnel, offering a novel perspective on the catalytic mechanisms of heme enzymes in nature. |
| format | Article |
| id | doaj-art-0b8e25cb1ddd4c078dffc8bf92926a8a |
| institution | Kabale University |
| issn | 2667-3703 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Engineering Microbiology |
| spelling | doaj-art-0b8e25cb1ddd4c078dffc8bf92926a8a2025-08-20T03:31:53ZengElsevierEngineering Microbiology2667-37032025-06-015210020710.1016/j.engmic.2025.100207Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesisYuanyuan Jiang0Zhong Li1Shengying Li2State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaDepartment of Chemistry, University of Basel, Basel 4002, SwitzerlandState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China; Corresponding author.Conventional heme enzymes utilize iron–oxygen intermediates to activate substrates and drive reactions. Recently, Chen et al. discovered a novel NADPH-independent superoxide mechanism of heme catalase EasC, which facilitates an O2-dependent radical oxidative cyclization reaction during ergot alkaloid biosynthesis. This enzyme coordinates superoxide-mediated catalysis by connecting spatially distinct NADPH-binding pocket and heme pocket via a slender tunnel, offering a novel perspective on the catalytic mechanisms of heme enzymes in nature.http://www.sciencedirect.com/science/article/pii/S2667370325000219Ergot alkaloidsHeme catalaseSuperoxideCooperative catalysisRadical oxidative cyclization |
| spellingShingle | Yuanyuan Jiang Zhong Li Shengying Li Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis Engineering Microbiology Ergot alkaloids Heme catalase Superoxide Cooperative catalysis Radical oxidative cyclization |
| title | Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| title_full | Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| title_fullStr | Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| title_full_unstemmed | Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| title_short | Superoxide-mediated O2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| title_sort | superoxide mediated o2 activation drives radical cyclization in ergot alkaloid biosynthesis |
| topic | Ergot alkaloids Heme catalase Superoxide Cooperative catalysis Radical oxidative cyclization |
| url | http://www.sciencedirect.com/science/article/pii/S2667370325000219 |
| work_keys_str_mv | AT yuanyuanjiang superoxidemediatedo2activationdrivesradicalcyclizationinergotalkaloidbiosynthesis AT zhongli superoxidemediatedo2activationdrivesradicalcyclizationinergotalkaloidbiosynthesis AT shengyingli superoxidemediatedo2activationdrivesradicalcyclizationinergotalkaloidbiosynthesis |