Journal of Biochemistry Advance Access originally published online on January 23, 2007
Journal of Biochemistry 2007 141(3):421-428; doi:10.1093/jb/mvm046
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© 2007 The Japanese Biochemical Society.
Cloning and Characterization of Ferredoxin and Ferredoxin-NADP+ Reductase from Human Malaria Parasite
1Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita; 2Department of Molecular Protozoology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan; and 3Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
*To whom correspondence should be addressed. Tel: +81-6-6879-8611, Fax: +81-6-6879-8613, E-mail: a-yoko{at}protein.osaka-u.ac.jp
Received December 1, 2006; Accepted January 17, 2007
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Abstract |
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The human malaria parasite (Plasmodium falciparum) possesses a plastid-derived organelle called the apicoplast, which is believed to employ metabolisms crucial for the parasite's survival. We cloned and studied the biochemical properties of plant-type ferredoxin (Fd) and Fd-NADP+ reductase (FNR), a redox system that potentially supplies reducing power to Fd-dependent metabolic pathways in malaria parasite apicoplasts. The recombinant P. falciparum Fd and FNR proteins were produced by synthetic genes with altered codon usages preferred in Escherichia coli. The redox potential of the Fd was shown to be considerably more positive than those of leaf-type and root-type Fds from plants, which is favourable for a presumed direction of electron flow from catabolically generated NADPH to Fd in the apicoplast. The backbone structure of P. falciparum Fd, as solved by X-ray crystallography, closely resembles those of Fds from plants, and the surface-charge distribution shows several acidic regions in common with plant Fds and some basic regions unique to this Fd. P. falciparum FNR was able to transfer electrons selectively to P. falciparum Fd in a reconstituted system of NADPH-dependent cytochrome c reduction. These results indicate that an NADPH–FNR–Fd cascade is operative in the apicoplast of human malaria parasites.
Key Words: ferredoxin, ferredoxin-NADP+ reductase, human malaria parasite, redox potential, X-ray crystallography
Abbreviations: cyt c, cytochrome c; Fd, ferredoxin; FNR, ferredoxin-NADP+ reductase; PfFd, P. falciparum Fd; PfFNR, P. falciparum FNR
Present address: Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8802, Japan
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