POR structural domains important for the enzyme activity in R. capsulatus complementation system.

摘要: NADPH:protochlorophyllide oxidoreductase (POR) catalyzes hydrogen transfer from NADPH to protochlorophyllide (PChlide) in the course of chlorophyll biosynthesis photosynthetic organisms and is involved regulation development apparatus higher plants, algae cyanobacteria. To approach molecular factors determining enzyme activity a living cell, several mutants POR pea (Pisum sativum) with site-directed modifications different parts were generated. The mutant enzymes expressed R. capsulatus deficient BChl biosynthesis, their catalytic ability integrate bacterial metabolism analyzed. Our results demonstrate that heterologous cell system, plant integrated porphyrin network its leads formation chlorophyll-proteins (CPs). study reveals domains important for association other subcellular components activity, including identification putative reaction center substrate binding site. also demonstrated an unknown structural factor photoactive complex etiolated plants. Moreover, our findings suggest might be directly porphyrins.