Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase.

@article{Brcker2010BiosynthesisO,
  title={Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase.},
  author={Markus Br{\"o}cker and Denise W{\"a}tzlich and Miguel Saggu and Friedhelm Lendzian and J{\"u}rgen Moser and Dieter Jahn},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 11},
  pages={8268-77}
}
Dark operative protochlorophyllide oxidoreductase (DPOR) catalyzes the light-independent two-electron reduction of protochlorophyllide a to form chlorophyllide a, the last common precursor of chlorophyll a and bacteriochlorophyll a biosynthesis. During ATP-dependent DPOR catalysis the homodimeric ChlL(2) subunit carrying a [4Fe-4S] cluster transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)(2), which also possesses a redox active [4Fe-4S] cluster. To… CONTINUE READING