Chloroplast Rieske Center. EPR study on its spectral characteristics, relaxation and orientation properties.

The spectral parameters, the orientation of the g tensor in two-dimensionally ordered multilayers and the relaxation properties of the Rieske center in purified cytochrome b6f complex from spinach were studied by EPR spectroscopy. A trough at g = 1.76 - 1.74 was unambiguously identified as the gx signal on the basis of the sensitivity of its field position to inhibitors and oxidized plastoquinone. In contrast to previous reports, the orientation of the chloroplast Rieske center was found to be identical to that of its cytochrome bc1 counterpart, provided that non-saturating EPR conditions were applied. Upon onset of microwave saturation, however, the orientation with respect to the ordered multilayers where the gy signal (g = 1.9) was maximal, changed drastically and was then similar to the orientation reported previously (Prince R. C., Crowder, M. S., and Bearden, A. J. (1980) Biochim. Biophys. Acta 592, 323-337). The unusually anisotropic saturation behavior of the EPR spectrum was characterized in detail, whereby hitherto controversial results on the spectral parameters of the chloroplast Rieske center could be rationalized. The observed phenomena are discussed on the basis of three tentative models which are able to qualitatively explain the effects.