Rubisco kinetic acclimation at the holoenzyme level
to confer a stabilizing effect to the active site relative to the cool temperature-expressed SSu. This increase in stability manifested as a reduction in flexibility and increase in substrate affinity, indicating that fine-tuning of local stability may underlie Rubisco kinetic acclimation.
Authors
- Stavros Azinas (ORCID: https://orcid.org/0000-0002-3744-9229)
- Bryce C. Askey (ORCID: https://orcid.org/0000-0002-4449-6891)
- Arthur D. Laganowsky (ORCID: https://orcid.org/0000-0001-5012-5547)
- Zhen Guo Oh (ORCID: https://orcid.org/0000-0002-1629-3368)
- Laura H. Gunn (ORCID: https://orcid.org/0000-0003-2072-0884)
- Maddie Ceminsky
- Yongsheng Wang
- Elena Scott
Institutions
- Stockholm University (SE)
- Cornell University (US)
- Science for Life Laboratory (SE)
- Carnegie Department of Plant Biology (US)
- Texas A&M University (US)
Publication Details
- Journal
- Proceedings of the National Academy of Sciences
- Published
- 2026-04-15
- DOI
- https://doi.org/10.1073/pnas.2519914123
- Citations
- 1
- Primary Topic
- Photosynthetic Processes and Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 13.33
Funders
- U.S. Department of Energy
- Welch Foundation
- National Institutes of Health