Oxidation-Reduction Potentials of Bound Iron-Sulfur Proteins of Photosystem I

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Digitonin - fractionated photosystem - I subchloroplasts were titrated potentiometrically between -450 and -610 mV at pH 10. Examination of the titrated subchloroplasts by low-temperature (13°K) electron paramagnetic resonance spectroscopy revealed resonances centered at values of 2.05, 1.94, 1.92, 1.89, and 1.86 on the g-factor scale. The peak heights depended on the potentials at which the chloroplasts were poised. The resonances of at least three iron-sulfur centers can be recognized: one with lines at g = 2.05 and 1.94; one with lines at g = 2.05, 1.92, and 1.89; and one for which only a line at g = 1.86 has been resolved. The midpoint potentials of the iron-sulfur species fall into two distinctly separate regions: the titration profile of the g = 1.94 signal, the first segment of the g = 2.05 plot, and the rise phase of the g = 1.86 signal had a value of -530 ± 5 mV; the upper segment of the g = 2.05 plot, the decrease phase of the g = 1.86 signal, and the g = 1.89 profile had a midpoint potential estimated to be [unk] -580 mV. The oxidation-reduction reaction of each of the bound iron-sulfur species, as represented by the changes of the electron paramagnetic resonance spectra, was reversible and apparently involved a two-electron change.

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