Inhomogeneity of the EPR multiline signal from the S-2-state of the photosystem II oxygen-evolving enzyme

The manganese complex (Mn-4) which is responsible for water oxidation in photosystem II is EPR detectable in the S-2-state, one of the five redox states of the enzyme cycle, The S-2-state is observable at 10 K either as an EPR multiline signal (spin S = 1/2) or as a signal at g = 4.1 (spin S = 3/2 or 5/2). It has recently been shown that the state responsible for the multiline signal is converted to that responsible for the g = 4.1 signal upon the absorption of near-infrared light [Boussac A, Girerd J-J, Rutherford AW (1996) Biochemistry 35:6983-6989]. It is shown here that the yield of the spin interconversion may be variable and depends on the photosystem II (PSII) preparations. The EPR multiline signal detected after near-infrared illumination, and which originates from PSII centers not susceptible to the near-infrared light, is shown to be different from that which originates from infrared-susceptible PSII centers, The total St-multiline signal results from the superposition of the two multiline signals which originate from these two PSII populations. One S-2 population gives rise to a ''narrow'' multiline signal characterized by strong central lines and weak outer lines. The second population gives rise to a ''broad'' multiline signal in which the intensity of the outer lines, at low and high field, are proportionally larger than those in the narrow multiline signal. The larger the relative amplitude of the outer lines at low and high field, the higher is the proportion of the near-infrared-susceptible PSII centers and the yield of the multiline to g = 4.1 signal conversion. This inhomogeneity of the EPR multiline signal is briefly discussed in terms of the structural properties of the Mn-4 complex.