Year-end Sale % OFF 
Abstract
The nature of proton transfer (PT) in proteins is explored by considering the catalytic cycle of carbonic anhydrase III. Special attention is paid to the free energy relationship established by Silverman and co-workers (Silverman, D. N.; Tu, C.; Chen, X.; Tanhauser, S. M.; Kresge, A. J.; Laipis, P. J. Biochemistry 1993, 34, 10757−10762). The free energy surfaces for the PT process is analyzed in the framework of the modified Marcus theory of Warshel and co-workers (Warshel, A.; Hwang, J. K.; Aqvist, J. Faraday Discuss. 1992, 93, 22), using realistic values of the relevant reorganization energy and the off-diagonal mixing term. It is found that the free energy relationship reflects a much more complex situation than that deduced from an empirical fit to the standard two-state Marcus formula. Apparently, the PT process involves three or more parabolic free energy surfaces rather than the two assumed in the Marcus treatment. Furthermore, PT processes involve large off-diagonal mixing terms that lead to appar...
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.
