Recent developments in biological water oxidation

Montserrat Pérez-Navarro, Frank Neese, Wolfgang Lubitz, Dimitrios A. Pantazis, Nicholas Cox*

*Corresponding author for this work

    Research output: Contribution to journalReview articlepeer-review

    93 Citations (Scopus)


    Rapid progress has been made in the last five years towards resolution of the structure of nature's water splitting catalyst - a Mn4O5Ca cofactor embedded in Photosystem II - especially in the field of X-ray crystallography. In addition, recent magnetic resonance data have allowed the structure of the cofactor to be accessed in its last metastable intermediate state, prior to O-O bond formation. This activated form of the catalyst is geometrically similar to that seen by X-ray crystallography, which represents the resting state of the cofactor, but requires the coordination of an additional water molecule to the cofactor, rendering all Mn ions six coordinate. Importantly, it locates two water derived, Mn bound oxygen ligands in close proximity. It is these two oxygen ligands that likely form the product O2 molecule, as proposed earlier by quantum chemical modeling. Current views on the molecular level events that facilitate catalyst activation, that is, catalyst/substrate deprotonation, Mn oxidation and water molecule insertion are briefly described.

    Original languageEnglish
    Pages (from-to)113-119
    Number of pages7
    JournalCurrent Opinion in Chemical Biology
    Publication statusPublished - 1 Apr 2016


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