This website uses cookies to give you the best user experience. If you continue without changing your settings we'll assume you are happy to receive all RSC cookies. You can change your cookie settings by navigating to our Privacy and Cookies page and following the instructions. These instructions are also obtainable from the privacy link at the bottom of any RSC page.
Lite Version|Standard version
Home > Chemical Communications >
To gain access to this content please
Log in via your home Institution.
Log in with your member or subscriber username and password.
Download


Buy PDF Add PDF to Basket (£42.50*)
*Exclusive of taxes
This article contains 3 page(s)
Abstract | Cited by

Multiple profiles for the reaction from chorismate to prephenate in the enzyme chorismate mutase calculated with hybrid density functional combined quantum mechanics/molecular mechanics methods (B3LYP/6-31G(d)–CHARMM27) agree well with experiment, and provide direct evidence of transition-state stabilization by this important enzyme, which is at the centre of current debates about the nature of enzyme catalysis.

Graphical abstract: Multiple high-level QM/MM reaction paths demonstrate transition-state stabilization in chorismate mutase: correlation of barrier height with transition-state stabilization

Page: ^ Top


Enter Keywords, author, title,reference, or DOI
Log in | Register