Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is an enzyme catalyzing carbon fixation reaction in photosynthesis with very low molecular activity. One of the effective ways of improving RuBisCO activity is the re-engineering by the mutation of amino acid residues. It is necessary for the rational re-engineering of RuBisCO to clarify the role of each amino acid residue. In this research, we carried out density functional theory calculations on the 22-residues-model around active site of RuBisCO, estimated rate-limiting step, and found 3 important amino acid residues that can greatly influence the reaction.
