Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum.
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.
Röhrich
René C
RC
Biochemisches Institut, Justus-Liebig-Universität Giessen, Friedrichstrasse 24, 35392 Giessen, Germany.
Englert
Nadine
N
Troschke
Katrin
K
Reichenberg
Armin
A
Hintz
Martin
M
Seeber
Frank
F
Balconi
Emanuela
E
Aliverti
Alessandro
A
Zanetti
Giuliana
G
Köhler
Uwe
U
Pfeiffer
Matthias
M
Beck
Ewald
E
Jomaa
Hassan
H
Wiesner
Jochen
J
D000818:Animals; D002384:Catalysis; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism*; D005288:Ferredoxins / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010269:Paraquat / Q000737:chemistry; D010963:Plasmodium falciparum / Q000201:enzymology*; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics; D013729:Terpenes / Q000378:metabolism*
D005288:Ferredoxins; D015800:Protozoan Proteins; D011994:Recombinant Proteins; D013729:Terpenes; D009249:NADP; D005287:Ferredoxin-NADP Reductase; D010269:Paraquat