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Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase

Nature Structural & Molecular Biology volume 10, pages 491–492 (2003)Cite this article

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Abstract

The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.

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Figure 1: Ultrafast reaction dynamics in POR.
Figure 2: SADS from a global analysis of the data using a sequential model.
Figure 3

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  • 19 May 2003

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Acknowledgements

D.J.H. and C.N.H. were supported by the BBSRC, UK. M.L.G. was supported by a NWO-ALW PULS fellowship.

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Authors and Affiliations

  1. Department of Molecular Biology and Biotechnology University of Sheffield, University of Sheffield, Sheffield, S10 2TN, UK

    Derren J Heyes & C Neil Hunter

  2. Department of Exact Sciences, Vrije Universiteit, Amsterdam, 1081 HV, The Netherlands

    Ivo H M van Stokkum, Rienk van Grondelle & Marie Louise Groot

Authors
  1. Derren J Heyes
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  2. C Neil Hunter
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  3. Ivo H M van Stokkum
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  4. Rienk van Grondelle
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  5. Marie Louise Groot
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Correspondence to C Neil Hunter.

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Heyes, D., Hunter, C., van Stokkum, I. et al. Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase. Nat Struct Mol Biol 10, 491–492 (2003). https://doi.org/10.1038/nsb929

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