Loss of the cytochrome b6f subunit PetN destabilizes the complex and severely impairs state transitions in Anabaena variabilis

The cytochrome b6f complex (Cyt b6f) plays pivotal roles in both linear and cyclic electron transport of oxygenic photosynthesis in plants and cyanobacteria. The 4 large subunits of Cyt b6f are responsible for organizing the electron transfer chain within Cyt b6f and have their counterparts in the cytochrome bc1 complex in other bacteria. The 4 small subunits of Cyt b6f are unique to oxygenic photosynthesis, and their functions remain to be elucidated. Here, we report that Cyt b6f was destabilized by the loss of PetN, one of the small subunits, in a petN mutant (Delta petN) of Anabaena variabilis ATCC 29413 and that the amount of the large subunits of Cyt b6f decreased to 20%-25% of that in the wild type (WT). The oxygen evolution activity of Delta petN was similar to 30% of that from the WT, and the activity could largely be restored by the addition of N,N,N ', N '-tetramethyl-p-phenylenediamine (TMPD), which functions as an electron carrier and bypasses Cyt b6f. Both linear and cyclic electron transfer of the mutant became partially insensitive to the Cyt b6f inhibitor 2,5-dibromo-3-methyl-6-isopropylbenzoquinone. Although the plastoquinone pool was largely reduced in Delta petN under normal light conditions, the mutant had a substantially higher PSII/PSI ratio than the WT. State transitions in Delta petN were abolished, as revealed by 77 K fluorescence spectra and room temperature fluorescence kinetics in the presence of TMPD. Our findings strongly suggest that Cyt b6f is required for state transitions in the cyanobacteria. The cytochrome b6f complex in the cyanobacterium Anabaena variabilis ATCC 29413 requires the small subunit PetN for stability and the complex's potential role in state transitions.