Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum.

نویسندگان

  • René C Röhrich
  • Nadine Englert
  • Katrin Troschke
  • Armin Reichenberg
  • Martin Hintz
  • Frank Seeber
  • Emanuela Balconi
  • Alessandro Aliverti
  • Giuliana Zanetti
  • Uwe Köhler
  • Matthias Pfeiffer
  • Ewald Beck
  • Hassan Jomaa
  • Jochen Wiesner
چکیده

In the malaria parasite Plasmodium falciparum isoprenoid precursors are synthesised inside a plastid-like organelle (apicoplast) by the mevalonate independent 1-deoxy-d-xylulose-5-phosphate (DOXP) pathway. The last reaction step of the DOXP pathway is catalysed by the LytB enzyme which contains a [4Fe-4S] cluster. In this study, LytB of P. falciparum was shown to be catalytically active in the presence of an NADPH dependent electron transfer system comprising ferredoxin and ferredoxin-NADP(+) reductase. LytB and ferredoxin were found to form a stable protein complex. These data suggest that the ferredoxin/ferredoxin-NADP(+) reductase redox system serves as the physiological electron donor for LytB in the apicoplast of P. falciparum.

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عنوان ژورنال:
  • FEBS letters

دوره 579 28  شماره 

صفحات  -

تاریخ انتشار 2005