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Publication Date
Summer 2025
Digital Publisher
Digital Commons at St. Mary's University
Collection
McNair Scholars Symposium
Keywords
Rubisco, enzyme, nuclear magnetic resonance, carbon fixation, intermediates
Description
Ribulose 1,5-bisphosphate carboxylase/oxygenase, or RuBisCO, is an enzyme which plays an essential role in carbon fixation and plant metabolism. While RuBisCO is considered the most abundant protein on the planet, its catalytic mechanism is still not completely understood. RuBisCO is notoriously slow and exhibits low specificity for CO2 over O2, leading to energetically wasteful photorespiration. Efforts to improve RuBisCO’s catalytic efficiency have been hindered due to an incomplete picture of key transient intermediates involved in the reaction. Acid quenched single turnover reaction experiments in combination with 13C and 31P Nuclear Magnetic Spectroscopy (NMR) offers a promising approach for the characterization of RuBisCO’s reaction pathway at a molecular level, including the detection of short-lived intermediates. In this study, we present an initial framework for applying NMR techniques to probe the RuBisCO catalytic pathway. We assess the feasability of detecting catalytic intermediates under varying experimental conditions, including cofactor availability and reaction time. Our preliminary data reveal both the promise and the technical challenges of this approach, including issues related to sensitivity, intermediate lifetimes, and sample conditions. While the direct observation of individual intermediates remains a target for future work, these findings demonstrate the potential of NMR as a tool for investigating RuBisCO’s catalytic mechanism and provide a technical foundation for future research aimed at the characterization of reaction intermediates.
Disciplines
Enzymes and Coenzymes | Plant Biology | Plants
Format
MOV
Medium
Video
Size or Duration
14 minutes 57 seconds
City
San Antonio, Texas
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
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