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J Biol Chem, Vol. 274, Issue 41, 29399-29405, October 8, 1999
From the Division of Enzymology, Institute for Protein Research,
Osaka University, Suita, Osaka, 565-0871, Japan and the
¶ Department of Applied Chemistry and Biochemistry, Faculty of
Engineering, Kumamoto University, Kurokami, Kumamoto,
860-0862, Japan
Plant-type ferredoxin (Fd), a [2Fe-2S]
iron-sulfur protein, functions as an one-electron donor to
Fd-NADP+ reductase (FNR) or sulfite reductase (SiR),
interacting electrostatically with them. In order to understand the
protein-protein interaction between Fd and these two different enzymes,
10 acidic surface residues in maize Fd (isoform III), Asp-27, Glu-30,
Asp-58, Asp-61, Asp-66/Asp-67, Glu-71/Glu-72, Asp-85, and Glu-93, were
substituted with the corresponding amide residues by site-directed
mutagenesis. The redox potentials of the mutated Fds were not markedly
changed, except for E93Q, the redox potential of which was more
positive by 67 mV than that of the wild type. Kinetic experiments
showed that the mutations at Asp-66/Asp-67 and Glu-93 significantly
affected electron transfer to the two enzymes. Interestingly, D66N/D67N was less efficient in the reaction with FNR than E93Q, whereas this
relationship was reversed in the reaction with SiR. The static interaction of the mutant Fds with each the two enzymes was analyzed by
gel filtration of a mixture of Fd and each enzyme, and by affinity chromatography on Fd-immobilized resins. The contributions of Asp-66/Asp-67 and Glu-93 were found to be most important for the binding to FNR and SiR, respectively, in accordance with the kinetic data. These results allowed us to map the acidic regions of Fd required
for electron transfer and for binding to FNR and SiR and demonstrate
that the interaction sites for the two enzymes are at least partly distinct.
Comparison of the Electrostatic Binding Sites on the Surface of
Ferredoxin for Two Ferredoxin-dependent Enzymes,
Ferredoxin-NADP+ Reductase and Sulfite Reductase
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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