IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms9488.html
   My bibliography  Save this article

Energetics of proton release on the first oxidation step in the water-oxidizing enzyme

Author

Listed:
  • Keisuke Saito

    (Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba
    The University of Tokyo
    Japan Science and Technology Agency (JST), PRESTO)

  • A. William Rutherford

    (Sir Ernst Chain Building, Imperial College London)

  • Hiroshi Ishikita

    (Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba
    The University of Tokyo)

Abstract

In photosystem II (PSII), the Mn4CaO5 cluster catalyses the water splitting reaction. The crystal structure of PSII shows the presence of a hydrogen-bonded water molecule directly linked to O4. Here we show the detailed properties of the H-bonds associated with the Mn4CaO5 cluster using a quantum mechanical/molecular mechanical approach. When O4 is taken as a μ-hydroxo bridge acting as a hydrogen-bond donor to water539 (W539), the S0 redox state best describes the unusually short O4–OW539 distance (2.5 Å) seen in the crystal structure. We find that in S1, O4 easily releases the proton into a chain of eight strongly hydrogen-bonded water molecules. The corresponding hydrogen-bond network is absent for O5 in S1. The present study suggests that the O4-water chain could facilitate the initial deprotonation event in PSII. This unexpected insight is likely to be of real relevance to mechanistic models for water oxidation.

Suggested Citation

  • Keisuke Saito & A. William Rutherford & Hiroshi Ishikita, 2015. "Energetics of proton release on the first oxidation step in the water-oxidizing enzyme," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9488
    DOI: 10.1038/ncomms9488
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms9488
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/ncomms9488?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yu Guo & Lanlan He & Yunxuan Ding & Lars Kloo & Dimitrios A. Pantazis & Johannes Messinger & Licheng Sun, 2024. "Closing Kok’s cycle of nature’s water oxidation catalysis," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9488. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.