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Science 14 April 2006:
Vol. 312. no. 5771, pp. 208 - 209
DOI: 10.1126/science.1127654
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Perspectives

BIOCHEMISTRY:
Enzyme Motions Inside and Out

Stephen J. Benkovic and Sharon Hammes-Schiffer

In one enzyme, short-range thermal motions are sufficient to explain the transfer of a hydrogen by tunneling--a transition through a classically forbidden energy state.

The authors are in the Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. E-mail: sjb1{at}psu.edu (S.J.B.), shs{at}chem.psu.edu (S.H.-S.)

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Evolutionary Basis for the Coupled-domain Motions in Thermus thermophilus Leucyl-tRNA Synthetase.
K. M. E. Weimer, B. L. Shane, M. Brunetto, S. Bhattacharyya, and S. Hati (2009)
J. Biol. Chem. 284, 10088-10099
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Nuclear Quantum Tunneling in the Light-activated Enzyme Protochlorophyllide Oxidoreductase.
D. J. Heyes, M. Sakuma, S. P. de Visser, and N. S. Scrutton (2009)
J. Biol. Chem. 284, 3762-3767
   Abstract »    Full Text »    PDF »
The mechanism of rate-limiting motions in enzyme function.
E. D. Watt, H. Shimada, E. L. Kovrigin, and J. P. Loria (2007)
PNAS 104, 11981-11986
   Abstract »    Full Text »    PDF »


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