An electron spin-polarized signal of the P800+A1(Q)- state in the homodimeric reaction center core complex of Heliobacterium modesticaldum.

The function of menaquinone as electron acceptor A 1 was identified by EPR in the purified type 1 homodimeric reaction center core complex (RC core) of an anoxygenic photosynthetic bacterium, Heliobacterium modesticaldum. After illumination of the RC core at 210 K in the absence and presence of dithionite, we detected the radical of a special pair of bacteriochlorophyll g molecules (P800 (+)) at g = 2.0033 and a quinone-type radical at g = 2.0062, respectively, at 14 K. Flash excitation of the dark-frozen RC core at 14 K induced two types of transient EPR signals, i.e., the P800 (+) radical that decayed with a time constant of 3.7 ms and a much faster decay component that showed the electron spin polarization (ESP) pattern of E/A (E, emission; A, absorption). The latter one was assigned to the P800 (+)F X (-) radical pair state. A new ESP signal that had an apparent A/E/A/E pattern extended to the lower-magnetic-field side was transiently induced by the flash excitation in the RC core that was preilluminated at 210 K in the presence of ascorbate and subsequently cooled to 14 K in the light. The 210 K preillumination of the RC core in the presence of dithionite led to accumulation of the dark stable semiquinone-type signal at g = 2.0062 and increased the intensity of the light-induced P800 triplet signal. Flash excitation at 14 K induced the smaller A/E/A/E-type signal that had the greater contribution of the lower-magnetic-field envelope. This ESP signal could thus be ascribed to the P800 (+)A 1 (-) radical pair. The kinetics and spectral shape of this ESP signal suggest that menaquinone serves as secondary electron acceptor A 1 with the molecular orientation of its ring being somewhat different from that of phylloquinone in photosystem I.