The water-oxidizing manganese complex bound to the proteins of photosystem II (PSII) was studied by X-ray absorption spectroscopy on PSII membrane particles. An extended range for collection of extended X-ray absorption fine-structure (EXAFS) data was used (up to 16.6Å−1). The EXAFS suggests the presence of two Mn–Mn distances close to 2.7Å (per Mn4Ca complex); the existence of a third Mn–Mn distance below 2.9Å is at least uncertain. Interestingly, a distance of 3.7Å is clearly resolved in the extended-range data and tentatively assigned to a Mn–Mn distance. Taking into account the above EXAFS results (inter alia), we present a model for the structure of the PSII manganese complex, which differs from previous atomic-resolution models. Emphasizing the hypothetical character, we propose for all semi-stable S-states: (i) a structure of the Mn4Ca(μ-O)n core, (ii) a model of the amino acid environment, and (iii) assignments of distinct Mn oxidation states to all the individual Mn ions. This specific working model may permit discussion, verification and invalidation of its various features in comparison with experimental and theoretical findings.
Keywords: photosynthetic oxygen evolution, photosynthesis, water oxidation, X-ray absorption spectroscopy
Abbreviations: EXAFS, extended X-ray absorption fine-structure; FT, Fourier transform; PSII, photosystem II; FTIR, Fourier-transform infrared (spectroscopy); YZ, Tyr160/161 of the D1 protein; XANES, X-ray absorption near-edge structure; XAS, X-ray absorption spectroscopy