category
Nature Catalysis
date
Mar 26, 2026
slug
status
Published
summary
通过解析NifEN蛋白的多结构态,揭示了FeMo辅因子前体接收、成熟和传递的隧道-开关协同机制,为理解固氮酶金属簇组装提供了关键结构依据。
tags
蛋白质组学
type
Post
📄 原文题目
Gating the nitrogenase cofactor
🔗 原文链接
💡 AI 核心解读
通过解析NifEN蛋白的多结构态,揭示了FeMo辅因子前体接收、成熟和传递的隧道-开关协同机制,为理解固氮酶金属簇组装提供了关键结构依据。
📝 英文原版摘要
<p>Nature Catalysis, Published online: 26 March 2026; <a href="https://www.nature.com/articles/s41929-026-01498-8">doi:10.1038/s41929-026-01498-8</a></p>Biological nitrogen fixation is vital for sustainable agriculture, yet nitrogenase engineering is hindered by limited insight into their essential metallocluster cofactor assembly and transfer. Here, by capturing the nitrogenase biosynthetic component NifEN in multiple structural states, a tunnel-and-switch mechanism that coordinates receipt, maturation and delivery of the FeMo-cofactor precursor is revealed.
- 作者:NotionNext
- 链接:https://tangly1024.com/article/33048bd6-1f96-817b-9b19-c1a4d638eb3f
- 声明:本文采用 CC BY-NC-SA 4.0 许可协议,转载请注明出处。
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