Skip Navigation



Journal of Biochemistry Advance Access published online on January 23, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm046
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
141/3/421    most recent
mvm046v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Kimata-Ariga, Y.
Right arrow Articles by Hase, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kimata-Ariga, Y.
Right arrow Articles by Hase, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society

Cloning and Characterization of Ferredoxin and Ferredoxin-NADP+ Reductase from Human Malaria Parasite

Yoko Kimata-Ariga1, Genji Kurisu2, Masami Kusunoki, Sayaka Aoki3, Dan Sato3, Tamaki Kobayashi4, Kiyoshi Kita4, Toshihiro Horii3 and Toshiharu Hase

Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan, 3Department of Molecular Protozoology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan, the 4Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
2Present address: Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8802, Japan.

1Address correspondence to: Yoko Kimata-Ariga, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan: Phone +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


  Abstract

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 favorable 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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
Y. Kimata-Ariga, T. Saitoh, T. Ikegami, T. Horii, and T. Hase
Molecular Interaction of Ferredoxin and Ferredoxin-NADP+ Reductase from Human Malaria Parasite
J. Biochem., December 1, 2007; 142(6): 715 - 720.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.