Last step of electron transport from ferredoxin to NADP+ in photosynthesis light reactions catalyses ferredoxin: NADP oxidoreductase (FNR). FNR is present as soluble protein in stroma, but also bound to the protein complexes on the membrane with thylakoid rhodanase-like protein (TROL) and translocon on the inner envelope chloroplast membrane (Tic62), which have identical C terminal FNR binding domain [1,2]. During the electron transport, FNR anchored by TROL protein transfers electrons on NADP+ and forms NADPH which is then used in Calvin cycle as reducing agent.
View Article and Find Full Text PDFInvestigations of the luminal immunophilin AtCYP38 (cyclophilin 38) in Arabidopsis thaliana (At), the orthologue of the complex immunophilin TLP40 from Spinacia oleracea, revealed its involvement in photosystem II (PSII) repair and assembly, biogenesis of PSII complex, and cellular signalling. However, the main physiological roles of AtCYP38 and TLP40 are related to regulation of thylakoid PP2A-type phosphatase involved in PSII core protein dephosphorylation, and chaperone function during protein folding. Here we further investigate physiological roles of AtCYP38 and analyse the ultrastructure of chloroplasts from cyp38-2 plants.
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