EMAIL THIS PAGE TO A FRIEND

Annual review of biochemistry

Hydrogen tunneling links protein dynamics to enzyme catalysis.


PMID 23746260

Abstract

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.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

295396
Hydrogen, ≥99.99%
H2
00473
Hydrogen, ≥99.999%
H2