A Fe2+ ion on the acceptor side of plant photosystem II has been substituted by Zn2+ and an anion radical of the primary acceptor quinone, Q−A, has been studied by electron spin echo method. The electron spin echo modulation shows the interaction of the unpaired electron of Q−A with nitrogen nuclei of the histidine and, probably, alanine residues situated nearby. The comparison of the modulation spectra of Q−A with those of the anion radical of plastoquinone-9 stabilized in protonated and deuterated isopropanol matrices allows one to distinguish between the spectrum lines due to the quinone protons and due to the protons of other molecules that form hydrogen bonds with the oxygen atoms of the quinones.

Articles you may be interested inRestricted orientational motion of nitroxides in molecular glasses: Direct estimation of the motional time scale basing on the comparative study of primary and stimulated electron spin echo decays J. Chem. Phys. 122, 094702 (2005); 10.1063/1.1856926Electron spin echo envelope modulation theory for high electron spin systems in weak crystal fieldThe electron spin echo envelope modulation spectra of the reduced primary acceptor quinone, Q A , in two preparations of plant photosystem II, have been studied. In one of these preparations the Fe 2ϩ ion in the quinone-iron complex has been substituted by diamagnetic Zn 2ϩ . In the other preparation this iron ion has been converted into the diamagnetic state using a potassium cyanide treatment. A comparative analysis of two-dimensional three-pulse electron spin echo envelope modulation spectra has shown similar structure of the binding site of Q A in both preparations. Two nitrogen nuclei have been found to contribute to the spectra in both preparations. One of these nitrogens is, most probably, an amino nitrogen in the imidazole ring of histidine 215 of the D2 protein. The other nitrogen has been assigned to the peptide group of alanine 261 of the D2 protein. The numerical simulations of the electron spin echo envelope modulation spectra have shown that both nitrogens are simultaneously bound to Q A .

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A '2+1' pulse sequence electron spin echo (ESE) method was applied to measure the dipole interactions between the tyrosine YD+ and QA- in Photosystem II (PS II). In a CN--treated PS II, QA- EPR signal was observed at g=2.0045 position, because the non-heme Fe(II) was converted into a low-spin (S=0) state. The radical pair of YD+QA- was trapped by illumination for 8 min at 273 K, followed by dark adaptation for 3 min and freezing into 77 K. By using a proton matrix ENDOR, these trapped radicals were confirmed to be YD+ and QA-, respectively. The distance between the radical pair was estimated from the dipole interaction constant fitted to the observed '2+1' ESE time profile. The distance of YD+-QA- is determined to be 38.8+/-1.1 A. The magnetic dipole interaction between YD+ and ChlZ+ was determined in a Tris-treated PS II in which ChlZ+ was generated by illumination at 200 K for 10 min. The YD+-ChlZ+ distance was estimated to be 29.4+/-0.5 A. Copyright 1998 Elsevier Science B.V.