Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051799 | FEBS Letters | 2005 | 6 Pages |
Abstract
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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Authors
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,