Molecular dynamics on rubisco, a key enzyme to photosynthesis
File(s)
Author(s)
Chen, Zhili
Type
Thesis
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a key enzyme in photosynthesis, catalyzing the primary step of carbon fixation. Despite its essential role, Rubisco’s inefficiency hinders efforts to improve crop yields. This thesis investigates Rubisco’s structural dynamics, regulatory mechanisms, allosteric properties, and post-translational modifications (PTMs) to identify strategies for engineering more efficient enzyme variants.
Chapter 2 employs molecular dynamics simulations to explore Rubisco’s stability and binding dynamics across different states, highlighting critical residues and interactions that maintain its catalytic mechanism. Chapter 3 further examines allosteric regulation using protein residue network models, revealing key residues associated with negative cooperativity and inefficiencies that can be targeted for improvement. Chapter 4 focuses on the role of PTMs, such as acetylation and methylation, demonstrating their significant impact on Rubisco’s kinetic properties and catalytic efficiency.
The findings contribute to the broader goal of enhancing photosynthetic efficiency through targeted enzyme engineering, offering insights that can be applied in crop improvement efforts. By integrating computational and experimental approaches, this research establishes a foundation for optimizing Rubisco, potentially boosting agricultural yields.
Chapter 2 employs molecular dynamics simulations to explore Rubisco’s stability and binding dynamics across different states, highlighting critical residues and interactions that maintain its catalytic mechanism. Chapter 3 further examines allosteric regulation using protein residue network models, revealing key residues associated with negative cooperativity and inefficiencies that can be targeted for improvement. Chapter 4 focuses on the role of PTMs, such as acetylation and methylation, demonstrating their significant impact on Rubisco’s kinetic properties and catalytic efficiency.
The findings contribute to the broader goal of enhancing photosynthetic efficiency through targeted enzyme engineering, offering insights that can be applied in crop improvement efforts. By integrating computational and experimental approaches, this research establishes a foundation for optimizing Rubisco, potentially boosting agricultural yields.
Version
Open Access
Date Issued
2024-09-25
Date Awarded
01/02/2025
License URL
Advisor
Gould, Ian
Barter, Laura
Publisher Department
Department of Chemistry
Publisher Institution
Imperial College London
Qualification Level
Doctoral
Qualification Name
Doctor of Philosophy (PhD)