Complex formation between ferredoxin and Synechococcus ferredoxin:nitrate oxidoreductase

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1608, Issue 2-3, 2004, Pages 155-162

  Hirasawa, Masakazu ^a   Rubio, Luis M ^b,d   Griffin, Jeannie L ^a   Flores, Enrique ^b   Herrero, Antonia ^b   Li, Jun ^a,e   Kim, Sung Kun ^a   Hurley, John K ^c   Tollin, Gordon ^c   Knaff, David B ^a  

^a TEXAS TECH UNIVERSITY   (United States)

^b UNIVERSITY OF SEVILLE   (Spain)

^c UNIVERSITY OF ARIZONA   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Electrostatic interaction; Ferredoxin binding; Nitrate reductase

Indexed keywords

FERREDOXIN; NITRATE; NITRATE REDUCTASE; NITRITE; PARAQUAT;

ABSORPTION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRICITY; ENZYME ACTIVITY; IONIC STRENGTH; NITROGEN FIXATION; NONHUMAN; PRIORITY JOURNAL; REDUCTION; SYNECHOCOCCUS;

ANABAENA; ANABAENA SP.; NOSTOC SP. PCC 7119; SYNECHOCOCCUS; SYNECHOCOCCUS ELONGATUS PCC 7942; SYNECHOCOCCUS FERREDOXIN; SYNECHOCOCCUS SP.; SYNECHOCOCCUS SP. PCC 6301;

EID: 10744222123     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.11.006     Document Type: Article

References (46)

1. Guerrero M.G., Vega J.M., Losada M. The assimilatory nitrate-reducing system and its regulation. Annu. Rev. Plant Physiol. 32:1981;169-204.
2. Knaff D.B. Ferredoxin and ferredoxin-dependent enzymes. Ort D.R., Yocum C.F. Oxygenic Photosynthesis: The Light Reactions. 1996;333-361 Kluwer Academic Publishing, Dordrecht.
3. Flores E., Herrero A. Assimilatory nitrogen metabolism and its regulation. Bryant D.A. The Molecular Biology of Cyanobacteria. 1994;487-517 Kluwer Academic Publishing, Dordrecht.
4. Okuhara H., Matsumura T., Fujita Y., Hase T. Cloning and inactivation of genes encoding ferredoxin- and NADH-dependent glutamate synthases in the cyanobacterium Plectonema boryanum. Imbalances in nitrogen and carbon assimilations caused by deficiency of the ferredoxin-dependent enzyme. Plant Physiol. 120:1999;33-41.
5. + reductase. Nat. Struct. Biol. 8:2001;117-121.
6. Morales R., Charon M.-H., Kachalova G., Serre L., Medina M., Gómez-Moreno C., Frey M. A redox-dependent interaction between two electron-transfer partners involved in photosynthesis. EMBO Rep. 11:2000;271-276.
7. A.J. Andriesse, H. Bakker, EMBL/GenBank/DDBJ accession number X74597 .
8. Rubio L.M., Herrero A., Flores E. A cyanobacterial narB gene encodes a ferredoxin-dependent nitrate reductase. Plant Mol. Biol. 30:1996;845-850.
9. Rubio L.M., Flores E., Herrero A. Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase. Photosynth. Res. 72:2002;13-26.
10. Hirasawa M., Knaff D.B. Interaction of ferredoxin-linked nitrite reductase with ferredoxin. Biochim. Biophys. Acta. 830:1985;173-180.
11. Tagawa K., Arnon D.I. Oxidation-reduction potentials and stoichiometry of electron transfer in ferredoxins. Biochim. Biophys. Acta. 153:1968;602-613.
12. + reductase: site-directed mutagenesis and laser flash photolysis. Biochemistry. 32:1993;9346-9354.
13. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:1976;248-254.
14. Manzano C., Candau P., Gómez-Moreno C., Remplio A.M., Losada M. Ferredoxin-dependent photosynthetic reduction of nitrate and nitrite by particles of Anacystis nidulans. Mol. Cell. Biochem. 10:1976;161-1169.
15. Mikami B., Ida S. Purification and properties of ferredoxin-nitrate reductase from the cyanobacterium Plectonema borynaum. Biochim. Biophys. Acta. 791:1984;294-304.
16. Hirasawa M., de Best J.H., Knaff D.B. The effect of lysine and arginine modifying reagents on spinach ferredoxin:nitrite oxidoreductase. Biochim. Biophys. Acta. 1140:1993;304-312.
17. Dose M.M., Hirasawa M., Kleis-SanFrancisco S., Lew E.L., Knaff D.B. Ferredoxin-binding site of ferredoxin:nitrite oxidoreductase. Differential chemical modification of the free enzyme and its complex with ferredoxin. Plant Physiol. 114:1997;1047-1053.
18. Hirasawa M., Knaff D.B. The role of lysine and arginine residues at the ferredoxin-binding site of spinach glutamate synthase. Biochim. Biophys. Acta. 1144:1993;85-91.
19. 5. Biochemistry. 18:1979;5422-5428.
20. Ida S., Mikami B. Purification and characterization of assimilatory nitrate reductase from the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 24:1983;649-658.
21. Matsubara H., Hase T. Phylogenetic consideration of ferredoxin in plants, particularly in algae. Jensen U., Fairbrothers D.E. Nucleic Acids in Plant Systematics. 1983;168-181 Springer-Verlag, Berlin.
22. Herrero A., Flores E., Guerrero M.G. Regulation of nitrate reductase cellular levels in the cyanobacteria Anabaena variabilis and Synechocystsis sp. FEMS Microbiol. Lett. 26:1985;21-25.
23. Shin M., San Pietro A. Complex formation of ferredoxin-NADP reductase with ferredoxin and with NADP. Biochem. Biophys. Res. Commun. 33:1968;38-42.
24. Foust G.P., Mayhew S.G., Massey V. Complex formation between ferredoxin triphosphopyridine nucleotide reductase and electron transfer proteins. J. Biol. Chem. 244:1969;964-970.
25. Nelson N., Neumann J. Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and partial some reactions. J. Biol. Chem. 244:1969;1932-1936.
26. Cammack R., Neumann J., Nelson N., Hall D.O. Circular dichroism studies of the complex between ferredoxin and ferredoxin-NADP reductase. Biochem. Biophys. Res. Commun. 42:1971;292-297.
27. +. Biochim. Biophys. Acta. 292:1973;13-19.
28. Knaff D.B., Smith J.M., Chain R.K. Circular dichroism studies of ferredoxin:protein complexes. Arch. Biochem. Biophys. 199:1980;117-122.
29. Hirasawa M., Boyer J.M., Gray K.A., Davis D.J., Knaff D.B. The interaction of ferredoxin with ferredoxin-linked chloroplast enzymes. Biochim. Biophys. Acta. 851:1986;23-28.
30. Hirasawa M., Droux M., Gray K.A., Boyer J.M., Davis D.J., Buchanan B.B., Knaff D.B. Ferredoxin-thioredoxin reductase: properties of its complex with ferredoxin. Biochim. Biophys. Acta. 935:1988;1-8.
31. Hirasawa M., Chang K.-T., Morrow K.J., Knaff D.B. Circular dichroism, binding and immunological studies on the interaction between spinach ferredoxin and glutamate synthase. Biochim. Biophys. Acta. 977:1989;150-156.
32. + and ferredoxin. J. Biol. Chem. 259:1984;8832-8839.
33. + oxidoreductase: the role of carboxyl groups, electrostatic surface potential and molecular dipole moment. Protein Sci. 2:1993;1126-1135.
34. + reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials. Protein Sci. 8:1999;1614-1620.
35. + reductase system from Anabaena. Biochimie. 80:1998;837-846.
36. + reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer. Arch. Biochem. Biophys. 312:1994;480-486.
37. Schmitz S., Böhme H. Amino acid residues involved in functional interaction of vegatative cell ferredoxin from the cyanobacterium Anabaena sp. PCC 7120 with ferredoxin:NADP reductase, nitrite reductase and nitrate reductase. Biochim. Biophys. Acta. 1231:1995;335-341.
38. Schmitz S., Navarro F., Kutzki C.K., Florencio F.J., Böhme H. Glutamate 94 of [2Fe-2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803. Biochim. Biophys. Acta. 1277:1996;135-140.
39. Aliverti A., Livraghi A., Piubelli L., Zanetti G. On the role of the acidic cluster Glu 92-94 of spinach ferredoxin I. Biochim. Biophys. Acta. 1342:1997;45-50.
40. Jacquot J.-P., Stein M., Suzuki A., Liottet S., Sandoz G., Miginiac-Maslow M. Residue Glu-91 of Chlamydomonas reinhardtii ferredoxin is essential for electron transfer to ferredoxin-thioredoxin reductase. FEBS Lett. 400:1997;293-296.
41. Hirasawa M., Hurley J.K., Salamon Z., Tollin G., Markley J.L., Chen H., Xia B., Knaff D.B. The role of aromatic and acidic amino acids in the electron transfer reaction catalyzed by spinach ferredoxin-dependent glutamate synthase. Biochim. Biophys. Acta. 1363:1998;134-146.
42. Boyd H., Leach S.J., Milligan B. N-acylsuccinimides as acylating agents for proteins: the selective acylation of lysine residues. Int. J. Pept. Protein Res. 4:1972;117-123.
43. Takahashi K. The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem. 243:1968;6171-6179.
44. García-Sánchez M.I., Díaz-Quintana A., Gotor C., Jacquot J.-P., de la Rosa M.A., Vega J.M. Homology predicted structure and functional interaction of ferredoxin from the eukaryotic alga Chlamydomonas reinhardtii with nitrite reductase and glutamate synthase. J. Biol. Inorg. Chem. 5:2000;713-719.
45. de Pascalis A.R., Schürmann P., Bosshard H.R. Comparison of the binding sites of plant ferredoxin for two ferredoxin-dependent enzymes. FEBS Lett. 337:1994;217-220.
46. + reductase and sulfite reductase. J. Biol. Chem. 274:1999;29399-29405.