Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.

ABSTRACT: Enzymes that catalyze long-range electron transfer (ET) reactions often function as higher order complexes that possess two structurally symmetrical halves. The functional advantages for such an architecture remain a mystery. Using cryoelectron microscopy we capture snapshots of the nitrogenase-like dark-operative protochlorophyllide oxidoreductase (DPOR) during substrate binding and turnover. DPOR catalyzes reduction of the C17 = C18 double bond in protochlorophyllide during the dark chlorophyll biosynthetic pathway. DPOR is composed of electron donor (L-protein) and acceptor (NB-protein) component proteins that transiently form a complex in the presence of ATP to facilitate ET. NB-protein is an α₂β₂ heterotetramer with two structurally identical halves. However, our

SUBMITTER: Kashyap R 

PROVIDER: S-EPMC12022308 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature