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In photosynthesis, final electron transfer from ferredoxin to NADP +  is accomplished by the flavo enzyme ferredoxin:NADP +  oxidoreductase (FNR). FNR is recruited to thylakoid membranes via integral membrane thylakoid rhodanase-like protein TROL. We address the fate of electrons downstream of photosystem I when TROL is absent. We have employed electron paramagnetic resonance (EPR) spectroscopy to study free radical formation and electron partitioning in TROL-depleted chloroplasts. DMPO was used to detect superoxide anion (O 2  .− ) formation, while the generation of other free radicals was monitored by Tiron. Chloroplasts from  trol  plants pre-acclimated to different light conditions consistently exhibited diminished O 2  .−  accumulation. Generation of other radical forms was elevated in  trol  chloroplasts in all tested conditions, except for the plants pre-acclimated to high-light. Remarkably, dark- and growth light-acclimated  trol  chloroplasts were resilient to O 2  .−  generation induced by methyl-viologen. We propose that the dynamic binding and release of FNR from TROL can control the flow of photosynthetic electrons prior to activation of the pseudo-cyclic electron transfer pathway.

TROL-FNR interaction reveals alternative pathways of electron partitioning in photosynthesis