Little is known about transient intermediates in photoinduced electron-transfer reactions of metalloproteins. Oxidative quenching of the triplet state of zinc cytochrome c, (3)Zncyt, is done at 20 degreesC, pH 7.00, and ionic strength of 1.00 M, conditions that suppress the thermal back-reaction and prolong the lifetime of the cation radical, Zncyt(+). This species is reduced by [Fe(CN)(6)](4-), [W(CN)(8)](4-), [Os(CN)(6)](4-), [Mo(CN)(8)](4-), and [Ru(CN)(6)](4-) complexes of similar structures and the same charge. The rate constants and thermodynamic driving forces for these five similar electron-transfer reactions were fitted to Marcus theory. The reorganization energy of Zncyt(+) is lambda = 0.38(5) eV, lower than that of native cytochrome c, because the redox orbital of the porphyrin cation radical is delocalized and possibly because Met80 is not an axial ligand to the zinc(II) ion in the reconstituted cytochrome c. The rate constant for electron self-exchange between Zncyt(+) and Zncyt, k(11) = 1.0(5) x 10(7) M-1 s(-1), is large owing to the extended electron delocalization and relatively low reorganization energy. These results may be relevant to zinc(II) derivatives of other heme proteins, which are often used in studies of photoinduced electron-transfer reactions.