Pyridoxine dehydrogenase <scp>SePdx</scp> regulates photosynthesis via an association with the phycobilisome in a cyanobacterium

Vitamin B6 (VitB6) deficiency is known to have a deleterious effect on photosynthesis, although the precise mechanism remains unclear. Pyridoxine dehydrogenase is a key protein involved in VitB6 biosynthesis, which facilitates the reversible reduction of pyridoxal (PL) and the oxidation of pyridoxine (PN), thereby contributing to VitB6 production. This study demonstrated the enzymatic activity of a pyridoxine dehydrogenase, SePdx, from the cyanobacterium Synechococcus elongatus PCC 7942 in the oxidation of PN. This protein is localized to the thylakoid membrane, interacts with components of the phycobilisome (PBS) and photosystem I (PSI), and plays a role in general stress responses. Deletion of sepdx leads to a distorted thylakoid membrane, shorter membrane spacing distances, and decreased phycobiliprotein content. Protein-protein interaction studies revealed interactions among SePdx, phycobiliprotein CpcA, and the PSI subunit PsaE. The structural analysis identified key residues that mediate SePdx-CpcA and SePdx-PsaE interactions, which were further confirmed through site-directed mutagenesis. Overall, the findings suggested that SePdx may influence PBS assembly, thereby establishing a link between VitB6 biosynthesis and photosynthesis.