Conformational changes in an ultrafast light-driven enzyme determine catalytic activity-Reference-Cited by-同舟云学术

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Conformational changes in an ultrafast light-driven enzyme determine catalytic activity

Published:2008-12 Issue:7224 Volume:456 Page:1001-1004
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Sytina Olga A.,Heyes Derren J.,Hunter C. Neil,Alexandre Maxime T.,van Stokkum Ivo H. M.,van Grondelle Rienk,Groot Marie Louise

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature07354.pdf

Reference31 articles.

1. Benkovic, S. J. & Hammes-Schiffer, S. A perspective on enzyme catalysis. Science 301, 1196–1202 (2003)

2. Villà, J. & Warshel, A. Energetics and dynamics of enzymatic reactions. J. Phys. Chem. B 105, 7887–7907 (2001)

3. Masgrau, L. et al. Atomic description of an enzyme reaction dominated by proton tunneling. Science 312, 237–241 (2006)

4. Kohen, A., Cannio, R., Bartolucci, S. & Klinman, J. P. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature 399, 496–499 (1999)

5. Eisenmesser, E. Z. et al. Intrinsic dynamics of an enzyme underlies catalysis. Nature 438, 117–121 (2005)

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