Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules
Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules
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DOI：
10.1038/s43247-023-00707-7
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发表时间：
2023-02
影响因子：
7.9
通讯作者：
A. Alsante;D. Thornton;S. Brooks
中科院分区：
文献类型：
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作者：
A. Alsante;D. Thornton;S. Brooks
大气气溶胶和云滴以及在其上生长的冰晶仍然是全球气候模型不确定性的主要来源。气溶胶的一个子集，冰成核粒子，在温度高于-38 °C时催化水滴的冻结。在这里，我们发现植物和浮游植物中最丰富的蛋白质之一RuBisCO是已知最有效的浸没冰成核颗粒之一，平均冻结温度为−7.9 ± 0.3 °C。此外，我们证明了RuBisCO存在于环境大陆气溶胶中，它可以作为冰成核颗粒。其他生物分子在−19 ° C至−26 °C的温度范围内充当浸没冰成核颗粒。此外，我们的研究结果表明，热变性不是冰成核颗粒蛋白质起源的通用指标，这表明目前的研究可能无法准确量化生物冰成核颗粒浓度及其全球重要性。
Atmospheric aerosol and the cloud droplets and ice crystals that grow on them remain major sources of uncertainty in global climate models. A subset of aerosol, ice nucleating particles, catalyze the freezing of water droplets at temperatures warmer than −38 °C. Here we show that RuBisCO, one of the most abundant proteins in plants and phytoplankton, is one of the most efficient known immersion ice nucleating particles with a mean freezing temperature of −7.9 ± 0.3 °C. Further, we demonstrate RuBisCO is present in ambient continental aerosol where it can serve as an ice nucleating particle. Other biogenic molecules act as immersion ice nucleating particles, in the range of −19 to −26 °C. In addition, our results indicate heat denaturation is not a universal indicator of the proteinaceous origin of ice nucleating particles, suggesting current studies may fail to accurately quantify biological ice nucleating particle concentrations and their global importance.