Rubisco, or ribulose-1,5-bisphosphate carboxylase/oxygenase, is one of the most important enzymes in photosynthesis, as it catalyzes the fixation of car-bon dioxide and thereby enables the production of sugars essential for plant growth and development. Despite its significance, Rubisco is relatively ineffi-cient due to its slow catalytic rate and low selectivity for carbon dioxide. Mo-reover, it can bind oxygen instead of carbon dioxide, leading to the formation of harmful compounds and energy loss. Structural and functional limitations of Rubisco have made it the focus of scientific efforts to improve its effici-ency for several decades. The main strategies to optimize its performance inc-lude directed evolution, heterologous expression, and the introduction of mechanisms to concentrate carbon dioxide within cells. Successful impro-vements in Rubisco activity could contribute to higher crop yields while si-multaneously reducing the environmental impact of agriculture. This thesis provides a comprehensive overview of key findings from previous research on the structure, composition, limitations, and functioning of Rubisco, as well as the approaches researchers are using to enhance its efficiency.
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