Carbon Dioxide Fixation in RuBisCO Is Protonation-State-Dependent and Irreversible
نویسندگان
چکیده
Most CO2 from the atmosphere is assimilated into photosynthetic organisms by ribulose 1,5-bisphosphate carboxylase-oxygenase (RuBisCO) enzyme as part of Calvin cycle. Despite its relevance and many efforts in last few decades, mechanistic picture catalytic fixation reaction still under debate. Here, we combine QM/MM molecular dynamics simulations with high-level electronic structure methods projector-embedding approach to provide reference values for activation free energies reaction. Our results show that carboxylation protonation-state-dependent irreversible, making reverse (decarboxylation reaction) highly unfavorable. The carbamylated lysine residue, Kcx201, coordinated magnesium(II) cation active site plays a central role shuffling protons substrate, creating proper reactive enolate species adds CO2. emerging microscopic involves several protonation equilibria free-energy profile provides insights may be used future improve enzymatic efficiency RuBisCO.
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ژورنال
عنوان ژورنال: ACS Catalysis
سال: 2022
ISSN: ['2155-5435']
DOI: https://doi.org/10.1021/acscatal.2c01677