NdhS interacts with cytochrome b₆f to form a complex in Arabidopsis

SUMMARY Cyclic electron transport (CET) around photosystem I (PSI) is crucial for photosynthesis to perform photoprotection and sustain the balance of ATP and NADPH. However, the critical component of CET, cyt b 6 f complex (cyt b 6 f ), functions in CET has yet to be understood entirely. In this study, we found that NdhS, a subunit of NADPH dehydrogenase‐like (NDH) complex, interacted with cyt b 6 f to form a complex in Arabidopsis. This interaction depended on the N‐terminal extension of NdhS, which was conserved in eukaryotic plants but defective in prokaryotic algae. The migration of NdhS was much more in cyt b 6 f than in PSI‐NDH super‐complex. Based on these results, we suggested that NdhS and NADP + oxidoreductase provide a docking domain for the mobile electron carrier ferredoxin to transfer electrons to the plastoquinone pool via cyt b 6 f in eukaryotic photosynthesis.