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The solid-state photo-CIDNP (photochemically induced dynamic nuclear polarization) effect allows for increase of signal and sensitivity in magic-angle spinning (MAS) NMR experiments. The effect occurs in photosynthetic reaction centers (RC) proteins upon illumination and induction of cyclic electron transfer. Here we show that the strength of the effect allows for observation of the cofactors forming the spin-correlated radical pair (SCRP) in isolated proteins, in natural photosynthetic membranes as well as in entire plants. To this end, we measured entire selectively  13 C isotope enriched duckweed plants ( Spirodela oligorrhiza ) directly in the MAS rotor. Comparison of  13 C photo-CIDNP MAS NMR spectra of photosystem II (PS2) obtained from different levels of RC isolation, from entire plant to isolated RC complex, demonstrates the intactness of the photochemical machinery upon isolation. The SCRP in PS2 is structurally and functionally very similar in duckweed and spinach ( Spinacia oleracea ). The analysis of the photo-CIDNP MAS NMR spectra reveals a monomeric Chl  a  donor. There is an experimental evidence for matrix involvement, most likely due to the axial donor histidine, in the formation of the SCRP. Data do not suggest a chemical modification of C-13 1  carbonyl position of the donor cofactor.

Photochemically induced dynamic nuclear polarization NMR on photosystem II: donor cofactor observed in entire plant