Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules

Alyssa N. Alsante; Daniel C.O. Thornton; Sarah D. Brooks

doi:10.1038/s43247-023-00707-7

Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules

Alyssa N. Alsante, Daniel C.O. Thornton, Sarah D. Brooks

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

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.

Original language	English
Article number	51
Journal	Communications Earth and Environment
Volume	4
Issue number	1
DOIs	https://doi.org/10.1038/s43247-023-00707-7
State	Published - Dec 2023
Externally published	Yes

Funding

Financial support was provided by NSF Atmospheric Chemistry Program (Award # AGS-2128133) to D.C.O.T. and S.D.B.. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the National Science Foundation. We thank Shawn M. Doyle and Jason B. Sylvan of the Department of Oceanography, Texas A&M University, for their guidance on RNA sample preparation and the use of the plate reader for RuBisCO quantification. The authors gratefully acknowledge the NOAA Air Resources Laboratory (ARL) for the provision of the HYSPLIT transport and dispersion model and READY website ( https://www.ready.noaa.gov ) used in this publication. Financial support was provided by NSF Atmospheric Chemistry Program (Award # AGS-2128133) to D.C.O.T. and S.D.B. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the National Science Foundation. We thank Shawn M. Doyle and Jason B. Sylvan of the Department of Oceanography, Texas A&M University, for their guidance on RNA sample preparation and the use of the plate reader for RuBisCO quantification. The authors gratefully acknowledge the NOAA Air Resources Laboratory (ARL) for the provision of the HYSPLIT transport and dispersion model and READY website (https://www.ready.noaa.gov) used in this publication.

Funders	Funder number
Department of Oceanography, Texas A&M University
NOAA Air Resources Laboratory
National Science Foundation	AGS-2128133
Army Research Laboratory

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abstract = "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.",

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AB - 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.

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Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules

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