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

@article{Sytina2008ConformationalCI,
  title={Conformational changes in an ultrafast light-driven enzyme determine catalytic activity},
  author={Olga A. Sytina and Derren J Heyes and C. Neil Hunter and Maxime T. A. Alexandre and Ivo H. M. van Stokkum and Rienk van Grondelle and Marie Louise Groot},
  journal={Nature},
  year={2008},
  volume={456},
  pages={1001-1004}
}
The role of conformational changes in explaining the huge catalytic power of enzymes is currently one of the most challenging questions in biology. Although it is now widely regarded that enzymes modulate reaction rates by means of short- and long-range protein motions, it is almost impossible to distinguish between conformational changes and catalysis. We have solved this problem using the chlorophyll biosynthetic enzyme NADPH:protochlorophyllide (Pchlide) oxidoreductase, which catalyses a… CONTINUE READING
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formation of the hydrogen-bonded intermediate state induced by hydrogen-bond strengthening

  • Zhao, G.-J., Han, K.-L. Site-specific solvation of the photoexcited protoc methanol
  • Biophys. J. 94, 38–46
  • 2008

Role of protein dynamics in reaction rate enhancement by enzymes

  • P. K. Agarwal
  • J. Am. Chem. Soc. 127,
  • 2005

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