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

Olga A. Sytina, Derren J. Heyes, C. Neil Hunter (), Maxime T. Alexandre, Ivo H. M. van Stokkum, Rienk van Grondelle and Marie Louise Groot
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Olga A. Sytina: Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands
Derren J. Heyes: Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
C. Neil Hunter: University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK
Maxime T. Alexandre: Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands
Ivo H. M. van Stokkum: Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands
Rienk van Grondelle: Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands
Marie Louise Groot: Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands

Nature, 2008, vol. 456, issue 7224, 1001-1004

Abstract: Enzyme catalysis: major contribution from conformational change (Hunter JF) Conformational changes involving short- and long-range protein motions contribute to the remarkable catalytic power of enzymes, but the extent of their contribution has been difficult to quantify. Sytina et al. have examined the chlorophyll biosynthetic enzyme NADPH:protochlorophyllide-oxidoreductase, which catalyses a light-driven reaction involving hydride and proton transfers. They show that prior excitation of the enzyme-substrate complex with a laser pulse induces a more favourable conformation of the active site and increases the catalytic efficiency of the coupled hydride and proton transfer reactions. Spectral changes in the mid-infrared following the absorption of one photon reveal significant conformational changes in the enzyme, illustrating the importance of flexibility and dynamics in the structure of enzymes for their function.

Date: 2008
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DOI: 10.1038/nature07354

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