Reconstitution of the Water-Oxidizing Complex in Manganese-Depleted Photosystem II Complexes by Using Synthetic Binuclear Manganese Complexes

S. I. Allakhverdiev, M. S. Karacan, G. Somer, N. Karacan, E. M. Khan, S. Y. Rane, S. Padhye, V. V. Klimov, G. Renger

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    35 Citations (Scopus)


    The efficiency of synthetic binuclear manganese complexes in reconstituting PS II electron flow and oxygen-evolution capacity was analyzed in PS II enriched preparations deprived of their manganese and of the extrinsic regulatory subunits. Measurements of the variable fluorescence induced by actinic illumination with continuous light led to the following results: (a) the synthetic binuclear complexes are more efficient than MnCl2 in establishing a PS II electron flow; (b) an almost complete restoration is achieved at concentrations of these complexes that correspond with an overall stoichiometry of two manganese per PS II; and (c) the electron flow restored by the binuclear manganese complexes closely resembles that of normal O2:-evolving PS II preparations in its resistance to addition of 50 μ EDTA, while that supported by MnCl2 is practically completely suppressed at the same chelator concentration. The rate of O2 evolution was used as a measure of the capability to function as manganese source in reconstitution of the oxygen evolution capacity. It was found that (i) as in the case of PS II electron transport, the synthetic binuclear manganese complexes are significantly more efficient than MnCl2; (ii) with respect to the manganese concentration, the maximum effect is achieved with a μ-oxo bridged binuclear Mn(III) complex (symbolized by M-3) at concentrations corresponding to four manganese per PS II; and (iii) at all concentrations of binuclear manganese complex M-3 a significantly higher restoration of the O2 evolution rate is achieved if the reconstitution assay contains in addition the extrinsic regulatory 33 kDa protein (PS II-O protein). The implications of these data are discussed in terms of electron donation and photoligation of the functional tetranuclear cluster of the water oxidase.

    Original languageEnglish
    Pages (from-to)12210-12214
    Number of pages5
    Issue number40
    Publication statusPublished - Oct 1 1994

    ASJC Scopus subject areas

    • Biochemistry


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