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Reconstitution of an apicoplast‐localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum
Author(s) -
Röhrich René C.,
Englert Nadine,
Troschke Katrin,
Reichenberg Armin,
Hintz Martin,
Seeber Frank,
Balconi Emanuela,
Aliverti Alessandro,
Zanetti Giuliana,
Köhler Uwe,
Pfeiffer Matthias,
Beck Ewald,
Jomaa Hassan,
Wiesner Jochen
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.10.037
Subject(s) - apicoplast , ferredoxin , plasmodium falciparum , plastid , reductase , ferredoxin thioredoxin reductase , biochemistry , biology , biosynthesis , thioredoxin reductase , electron transfer , organelle , chemistry , stereochemistry , enzyme , thioredoxin , malaria , photochemistry , gene , chloroplast , immunology
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 .