First published online December 18, 2003; 10.1104/pp.103.032755
Plant Physiology 134:255-264 (2004)
© 2004 American Society of Plant Biologists
BIOENERGETICS AND PHOTOSYNTHESIS
A Post Genomic Characterization of Arabidopsis Ferredoxins1
Guy Thomas Hanke*,
Yoko Kimata-Ariga,
Isao Taniguchi and
Toshiharu Hase
Division of Enzymology, Osaka University, 3–2 Yamadaoka, Suita, Osaka 565–0871, Japan (G.T.H., Y.K.-A., T.H.); and Department of Applied Chemistry and Biochemistry, Kumammoto University, 2–39–1 Kurokami 860–8555, Japan (I.T.)
In higher plant plastids, ferredoxin (Fd) is the unique soluble electron carrier protein located in the stroma. Consequently, a wide variety of essential metabolic and signaling processes depend upon reduction by Fd. The currently available plant genomes of Arabidopsis and rice (Oryza sativa) contain several genes encoding putative Fds, although little is known about the proteins themselves. To establish whether this variety represents redundancy or specialized function, we have recombinantly expressed and purified the four conventional [2Fe-2S] Fd proteins encoded in the Arabidopsis genome and analyzed their physical and functional properties. Two proteins are leaf type Fds, having relatively low redox potentials and supporting a higher photosynthetic activity. One protein is a root type Fd, being more efficiently reduced under nonphotosynthetic conditions and supporting a higher activity of sulfite reduction. A further Fd has a remarkably positive redox potential and so, although redox active, is limited in redox partners to which it can donate electrons. Immunological analysis indicates that all four proteins are expressed in mature leaves. This holistic view demonstrates how varied and essential soluble electron transfer functions in higher plants are fulfilled through a diversity of Fd proteins.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.032755.
1 This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (15G50320).
* Corresponding author; e-mail enzyme{at}protein.osaka-u.ac.jp; fax 81–6–6879–8613.
Received September 8, 2003;
returned for revision September 30, 2003;
accepted October 12, 2003.
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