马克斯普朗克海洋微生物研究所的研究团队发现，深海古菌Methanocaldococcus infernus产生的固氮酶具有非凡的耐热性能，在90℃以上的高温条件下仍能继续进行氮固定 1。该固氮酶蛋白在90℃开始分解，即使达到98℃时仍有部分保持完整 1。
这种固氮酶在分子结构上兼具多重特征，是已知最简单的固氮酶，却同时结合了钼基、钒基和铁基三种固氮酶的结构特征 1。研究人员首次在钼基固氮酶中观测到此前仅在钒基和铁基固氮酶中发现的"周转"状态 1。
与此相比，传统工业肥料生产采用的哈伯-博世工艺需要消耗大量能源，并与温室气体排放密切相关 1。该研究成果已发表在《自然通讯》2026年第17卷第1期 1。
Researchers at the Max Planck Institute for Marine Microbiology have identified an exceptionally heat-resistant enzyme produced by the deep-sea archaeon Methanocaldococcus infernus1. The nitrogenase enzyme maintains its ability to fix nitrogen at temperatures above 90°C, a remarkable property that sets it apart from most known proteins1. While nitrogenase proteins typically begin to break down at 90°C, portions of this enzyme remain structurally intact even at 98°C1.
The enzyme represents a unique convergence of structural features, combining characteristics found in molybdenum-based, vanadium-based, and iron-based nitrogenases—making it the simplest nitrogenase known to date1. The research team made the first-ever observation of a "turnover" state in a molybdenum-based nitrogenase, a condition previously detected only in vanadium-based and iron-based variants1. These findings, published in Nature Communications in 2026 (Volume 17, Issue 1), suggest the enzyme may represent ancestral characteristics shared by ancient nitrogenases1.
The discovery carries implications for biotechnology and sustainable agriculture. Current industrial fertilizer production relies on the energy-intensive Haber-Bosch process, which is associated with significant greenhouse gas emissions1. Understanding this heat-tolerant enzyme could inform the development of more efficient biological approaches to nitrogen fixation.
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