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Probing coupled motions in enzymatic hydrogen tunnelling reactions

Allemann, Rudolf Konrad, Evans, Rhiannon Mari and Loveridge, Edric Joel 2009. Probing coupled motions in enzymatic hydrogen tunnelling reactions. Biochemical Society Transactions 37 , pp. 349-353. 10.1042/BST0370349

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Abstract

Much work has gone into understanding the physical basis of the enormous catalytic power of enzymes over the last 50 years or so. Nevertheless, the detailed mechanism used by Nature's catalysts to speed chemical transformations remains elusive. DHFR (dihydrofolate reductase) has served as a paradigm to study the relationship between the structure, function and dynamics of enzymatic transformations. A complex reaction cascade, which involves rearrangements and movements of loops and domains of the enzyme, is used to orientate cofactor and substrate in a reactive configuration from which hydride is transferred by quantum mechanical tunnelling. In the present paper, we review results from experiments that probe the influence of protein dynamics on the chemical step of the reaction catalysed by TmDHFR (DHFR from Thermotoga maritima). This enzyme appears to have evolved an optimal structure that can maintain a catalytically competent conformation under extreme conditions.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Cardiff Catalysis Institute (CCI)
Subjects: Q Science > QD Chemistry
Uncontrolled Keywords: dihydrofolate reductase (DHFR), hydrogen tunnelling reaction, quantum mechanical tunnelling, protein-coupled motion, protein dynamics, Thermotoga maritima
Publisher: Biochemical Society
ISSN: 0300-5127
Funders: BBSRC
Last Modified: 05 Jun 2017 02:09
URI: http://orca.cf.ac.uk/id/eprint/5838

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