Temporally Overlapped but Uncoupled Motions in Dihydrofolate
Reductase Catalysis
- Publication date
- Publisher
Abstract
Temporal correlations between protein motions and enzymatic reactions
are often interpreted as evidence for catalytically important motions.
Using dihydrofolate reductase as a model system, we show that there
are many protein motions that temporally overlapped with the chemical
reaction, and yet they do not exhibit the same kinetic behaviors (KIE
and pH dependence) as the catalyzed chemical reaction. Thus, despite
the temporal correlation, these motions are not directly coupled to
the chemical transformation, and they might represent a different
part of the catalytic cycle or simply be the product of the intrinsic
flexibility of the protein