Higher order structure contributes to specific differences in redox potential and electron transfer efficiency of root and leaf ferredoxins

Biochemistry

Volumn 45, Issue 48, 2006, Pages 14389-14396

  Gou, Ping ^a,c   Hanke, Guy T ^a   Kimata Ariga, Yoko ^a   Standley, Daron M ^a   Kubo, Atsushi ^b   Taniguchi, Isao ^b   Nakamura, Haruki ^a   Hase, Toshiharu ^a  

^a OSAKA UNIVERSITY   (Japan)

^b KUMAMOTO UNIVERSITY   (Japan)

^c XINJIANG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL METHODS; ELECTRON TRANSPORT PROPERTIES; MOLECULAR STRUCTURE; PHOTOSYNTHESIS; PLANTS (BOTANY); TISSUE;

ELECTRON CASCADES; ELECTRON TRANSFERS; RECOMBINANT CHIMERAS; REDOX POTENTIAL;

PROTEINS;

FERREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; CALCULATION; CHIMERA; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME BINDING; MOLECULAR MODEL; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PLANT LEAF; PLANT ROOT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; WILD TYPE;

AMINO ACID SEQUENCE; ARABIDOPSIS; CHEMISTRY, PHYSICAL; CHROMATOGRAPHY, AFFINITY; ELECTRON TRANSPORT; FERREDOXINS; GENE EXPRESSION; IRON; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; PHYLOGENY; PLANT LEAVES; PLANT ROOTS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SULFUR;

EMBRYOPHYTA;

EID: 33845315087     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061779d     Document Type: Article

References (26)

1. Cammack, R., Rao, K. K., Bargeron, C. P., Hutson, K. G., Andrew, P. W., and Rogers, L. J. (1977) Midpoint redox potentials of plant and algal ferredoxins, Biochem. J. 168, 205-9.
2. Arnon, D. I. (1988) The discovery of ferredoxin: the photosynthetic path, Trends Biochem. Sci. 13, 30-3.
3. Knaff, D. (1996) Ferredoxin and ferredoxin dependent enzymes, in Oxygenic photosynthesis: The light reactions (Ort, D., and Yocum, C., Eds.) pp 333-361, Kluwer Academic Publishers, Dordrecht.
4. Suzuki, A., Oaks, A., Jacquot, J. P., Vidal, J., and Gadal, P. (1985) An Electron Transport System in Maize Roots for Reactions of Glutamate Synthase and Nitrite Reductase: Physiological and Immunochemical Properties of the Electron Carrier and Pyridine Nucleotide Reductase, Plant Physiol. 78, 374-378.
5. Hase, T., Kimata, Y., Yonekura, K., Matsumura, T., and Sakakibara, H. (1991) Molecular Cloning and Differential Expression of the Maize Ferredoxin Gene Family, Plant Physiol. 96, 77-83.
6. Wada, K., Onda, M., and Matsubara, H. (1986) Ferredoxin isolated from plant non-photosynthetic tissues: purification and characterization, Plant Cell Physiol. 27, 407-415.
7. Onda, Y., Matsumura, T., Kimata-Ariga, Y., Sakakibara, H., Sugiyama, T., and Hase, T. (2000) Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins, Plant Physiol. 123, 1037-45.
8. Hanke, G. T., Kimata-Ariga, Y., Taniguchi, I., and Hase, T. (2004) A post genomic characterization of Arabidopsis ferredoxins, Plant Physiol. 134, 255-64.
9. Akashi, T., Matsumura, T., Ideguchi, T., Iwakiri, K., Kawakatsu, T., Taniguchi, I., and Hase, T. (1999) Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase, J. Biol. Chem. 274, 29399-405.
10. Okutani, S., Hanke, G. T., Satomi, Y., Takao, T., Kurisu, G., Suzuki, A., and Hase, T. (2005) Three maize leaf ferredoxin: NADPH oxidoreductases vary in subchloroplast location, expression, and interaction with ferredoxin, Plant Physiol. 139, 1451-9.
11. Yonekura-Sakakibara, K., Onda, Y., Ashikari, T., Tanaka, Y., Kusumi, T., and Hase, T. (2000) Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize, Plant Physiol. 122, 887-94.
12. Taniguchi, I., Miyahara, A., Iwakiri, K., Hirakawa, Y., Hayashi, Y., Nishiyama, K., Akashi, T., and Hase, T. (1997) Electrochemical study of biological functions of particular evolutionary conserved amino acid residues using mutated molecules of maize ferredoxin, Chem. Lett. 1977, 929-30.
13. + reductase, Biochemistry 36, 15109-17.
14. Weber-Main, A. M., Hurley, J. K., Cheng, H., Xia, B., Chae, Y. K., Markley, J. L., Martinez-Julvez, M., Gomez-Moreno, C., Stankovich, M. T., and Tollin, G. (1998) An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop, Arch. Biochem. Biophys. 355, 181-8.
15. Hurley, J. K., Weber-Main, A. M., Stankovich, M. T., Benning, M. M., Thoden, J. B., Vanhooke, J. L., Holden, H. M., Chae, Y. K., Xia, B., Cheng, H., Markley, J. L., Martinez-Julvez, M., Gomez-Moreno, C., Schmeits, J. L., and Tollin, G. (1997) Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants, Biochemistry 36, 11100-17.
16. Pizzitutti, F., Serif, P., and Marchi, M. (2003) Theoretical investigation of the "CO in"-"CO out" isomerization in a [2Fe-2S] ferredoxin: free energy profiles and redox states, J. Am. Chem. Soc. 125, 15224-32.
17. Kurisu, G., Kusunoki, M., Katoh, E., Yamazaki, T., Teshima, K., Onda, Y., Kimata-Ariga, Y., and Hase, T. (2001) Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase, Nat. Struct. Biol. 8, 117-21.
18. Hanke, G. T., Kurisu, G., Kusunoki, M., and Hase, T. (2004) Fd: FNR electron transfer complexes: evolutionary refinement of structural interactions, Photosynth. Res. 81, 317-327.
19. Hurley, J. K., Hazzard, J. T., Martinez-Julvez, M., Medina, M., Gomez-Moreno, C., and Tollin, G. (1999) Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+ reductase: site-specific mutagen-esis, transient kinetic measurements, and electrostatic surface potentials, Protein Sci. 8, 1614-22.
20. Binda, C., Coda, A., Aliverti, A., Zanetti, G., and Mattevi, A. (1998) Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution, Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 1353-8.
21. Shen, B., Jollie, D. R., Stout, C. D., Diller, T. C., Armstrong, F. A., Gorst, C. M., La Mar, G. N., Stephens, P. J., and Burgess, B. K. (1994) Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential, J. Biol. Chem. 269, 8564-75.
22. Kimata, Y., and Hase, T. (1989) Localization of Ferredoxin Isoproteins in Mesophyll and Bundle Sheath Cells in Maize Leaf, Plant Physiol. 89, 1193-1197.
23. Standley, D. M., Toh, H., and Nakamura, H. (2005) GASH: an improved algorithm for maximizing the number of equivalent residues between two protein structures, BMC Bioinformatics 6, 221.
24. Morikami, K., Nakai, T., Kidera, A., Saito, M., and Nakamura, H. (1992) Presto(protein engineering simulator): A vectorized molecular mechanics program for biopolymers, Comput. Chem. 16, 243-8.
25. Standley, D. M., Toh, H., and Nakamura, H. (2004) Detecting local structural similarity in proteins by maximizing number of equivalent residues, Proteins 57, 381-91.
26. Lelong, C., Setif, P., Lagoutte, B., and Bottin, H. (1994) Identification of the amino acids involved in the functional interaction between photosystem I and ferredoxin from Synechocystis sp. PCC 6803 by chemical cross-linking, J. Biol. Chem. 269, 10034-9.