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Quantum chemical modeling of the kinetic isotope effect of the carboxylation step in RuBisCO

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons58585

Götze,  J. P.
Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Götze, J. P., & Saalfrank, P. (2012). Quantum chemical modeling of the kinetic isotope effect of the carboxylation step in RuBisCO. Journal of Molecular Modeling, 18(5), 1877-1883. doi:10.1007/s00894-011-1207-0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-ED41-3
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the most important enzyme for the assimilation of carbon into biomass, features a well-known isotope effect with regards to the CO2 carbon atom. This kinetic isotope effect α = k12/k13 for the carboxylation step of the RuBisCO reaction sequence, and its microscopic origin, was investigated with the help of cluster models and quantum chemical methods [B3LYP/6-31G(d,p)]. We use a recently proposed model for the RuBisCO active site, in which a water molecule remains close to the reaction center during carboxylation of ribulose-1,5-bisphosphate [B. Kannappan, J.E. Gready, J. Am. Chem. Soc. 130 (2008), 15063]. Alternative active-site models and/or computational approaches were also tested. An isotope effect alpha for carboxylation is found, which is reasonably close to the one measured for the overall reaction, and which originates from a simple frequency shift of the bending vibration of 12CO2 compared to 13CO2. The latter is the dominant mode for the product formation at the transition state.