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Plant Physiol, July 2000, Vol. 123, pp. 1037-1046
Differential Interaction of Maize Root
Ferredoxin:NADP+ Oxidoreductase with Photosynthetic and
Non-Photosynthetic Ferredoxin Isoproteins1
Yayoi
Onda,*
Tomohiro
Matsumura,2
Yoko
Kimata-Ariga,
Hitoshi
Sakakibara,
Tatsuo
Sugiyama, and
Toshiharu
Hase
Division of Enzymology, Institute for Protein Research, Osaka
University, 3-2 Yamadaoka, Suita, Osaka, 565-0871 Japan (Y.O., T.M.,
Y.K.-A., T.H.); and Department of Biological Mechanisms and Functions,
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya,
464-8601 Japan (H.S., T.S.)
In higher plants ferredoxin (Fd):NADP+ oxidoreductase
(FNR) and Fd are each distributed in photosynthetic and
non-photosynthetic organs as distinct isoproteins. We have cloned cDNAs
for leaf FNR (L-FNR I and L-FNR II) and root FNR (R-FNR) from maize
(Zea mays L.), and produced recombinant L-FNR I and
R-FNR to study their enzymatic functions through kinetic and Fd-binding
analyses. The Km value obtained by assay for
a diaphorase activity indicated that R-FNR had a 10-fold higher
affinity for NADPH than L-FNR I. When we assayed for NADPH-cytochrome
c reductase activity using maize photosynthetic Fd (Fd
I) and non-photosynthetic Fd (Fd III), the R-FNR showed a marked
difference in affinity between these two Fd isoproteins; the
Km for Fd III was 3.0 µM and
that for Fd I was 29 µM. Consistent with this, the
dissociation constant for the R-FNR:Fd III complex was 10-fold smaller
than that of the R-FNR:Fd I complex. This differential binding capacity
was confirmed by an affinity chromatography of R-FNR on Fd-sepharose with stronger binding to Fd III. L-FNR I showed no such differential interaction with Fd I and Fd III. These data demonstrated that R-FNR
has the ability to discriminate between these two types of Fds. We
propose that the stronger interaction of R-FNR with Fd III is crucial
for an efficient electron flux of NADPH-FNR-Fd cascade, thus supporting
Fd-dependent metabolism in non-photosynthetic organs.
1
This work was supported in part by a
Grant-in-Aid for the Encouragement of Young Scientists (no. 5145 to
Y.O.) and by Grants-in-Aid for Research on Priority Areas (nos. 9274101 and 09274102 to T.S. and 9274101 and 09274103 to T.H.) from the
Ministry of Education, Science and Culture of Japan.
2
Present address: Department of Biochemistry and
Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku,
Tokyo, 113-8602 Japan.
*
Corresponding author; e-mail enzyme{at}protein.osaka-u.ac.jp; fax
81-6-6879-8613.
© 2000 American Society of Plant Physiologists
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