One of the most controversial questions in enzymology today is whether protein dynamics are significant in enzyme catalysis. A particular issue in these debates is the unusual temperature-dependence of some kinetic isotope effects for enzyme-catalysed reactions. In the present paper, we review our recent model [Glowacki, Harvey and Mulholland (2012) Nat. Chem. 4, 169–176] that is capable of reproducing intriguing temperature-dependences of enzyme reactions involving significant quantum tunnelling. This model relies on treating multiple conformations of the enzyme–substrate complex. The results show that direct ‘driving’ motions of proteins are not necessary to explain experimental observations, and show that enzyme reactivity can be understood and accounted for in the framework of transition state theory.
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June 2012
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Conference Article|
May 22 2012
Protein dynamics and enzyme catalysis: the ghost in the machine?
David R. Glowacki;
David R. Glowacki
1
1Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.
1Correspondence may be addressed to either of these authors (emailDavid.R.Glowacki@bristol.ac.uk or Adrian.Mulholland@bristol.ac.uk).
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Jeremy N. Harvey;
Jeremy N. Harvey
1Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.
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Adrian J. Mulholland
Adrian J. Mulholland
1
1Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.
1Correspondence may be addressed to either of these authors (emailDavid.R.Glowacki@bristol.ac.uk or Adrian.Mulholland@bristol.ac.uk).
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Publisher: Portland Press Ltd
Received:
February 24 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem Soc Trans (2012) 40 (3): 515–521.
Article history
Received:
February 24 2012
Citation
David R. Glowacki, Jeremy N. Harvey, Adrian J. Mulholland; Protein dynamics and enzyme catalysis: the ghost in the machine?. Biochem Soc Trans 1 June 2012; 40 (3): 515–521. doi: https://doi.org/10.1042/BST20120047
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