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2013 ; 82
(ä): 471-96
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Hydrogen tunneling links protein dynamics to enzyme catalysis
#MMPMID23746260
Klinman JP
; Kohen A
Annu Rev Biochem
2013[]; 82
(ä): 471-96
PMID23746260
show ga
The relationship between protein dynamics and function is a subject of
considerable contemporary interest. Although protein motions are frequently
observed during ligand binding and release steps, the contribution of protein
motions to the catalysis of bond making/breaking processes is more difficult to
probe and verify. Here, we show how the quantum mechanical hydrogen tunneling
associated with enzymatic C-H bond cleavage provides a unique window into the
necessity of protein dynamics for achieving optimal catalysis. Experimental
findings support a hierarchy of thermodynamically equilibrated motions that
control the H-donor and -acceptor distance and active-site electrostatics,
creating an ensemble of conformations suitable for H-tunneling. A possible
extension of this view to methyl transfer and other catalyzed reactions is also
presented. The impact of understanding these dynamics on the conceptual framework
for enzyme activity, inhibitor/drug design, and biomimetic catalyst design is
likely to be substantial.
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