Abstract

ing to only 13% of total Cyt 6-559 in spinach chloroplasts, is analyzed with the help of a highly selective, computercontrolled spectrophotometer, which simultaneously applies 16 pulse modulated narrow band measuring beams with wavelengths in the cytochrome a-band (500-600 nm) for recordings of time resolved difference spectra. This Cyt 6-559 fraction remains oxidized upon dark incubation with ascorbate and is reduced upon illumination. It can be reduced by cyclic PSI in an antimycin A-sensitive reaction or in the course of antimycin A-insensitive linear electron transport via the Cyt b6/f complex. Reduction by NADPH in the dark requires ferredoxin. Simultaneous recordings of Cyt 6-563 and Cyt/ reveal close kinetic connection between this Cyt 6-559 fraction and the low potential chain of the Cyt 6 6 // complex. These results confirm and extend previous observations of Miyake et al. 1995 (Plant Cell Physiol. 36: 743) in maize mesophyll thylakoids, which led to the hypothesis that Cyt 6-559 (Fd) occupies the position of the postulated ferredoxin-plastoquinone reductase (FQR) in cyclic electron transport.

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