Abstract
The deprotonation of zinc-bound water in carbonic anhydrase II is the rate-limiting step in the catalytic reaction of CO2-bicarbonate conversion. In order to understand the factors determining the pKa of the zinc bound water at the active site, quantum chemistry calculation together with continuum model is carried out. The pka changes due to the active site mutation are well reproduced. Additionally, the structural analysis and charge/dipole examination provide evidence that the fluctuation of the active site structure and the redistribution of the electrostatics lead to the pKa shift. Also, the distinct pka value of the same type of mutation at different site results from asymmetric ligation and different electronic environment around the zinc ion. This study not only provides insight into the molecular mechanism of the enzyme but also helps design artificial material for CO2 sequestration.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
