Advertisement

Ferredoxin and Ferredoxin-Dependent Enzymes

  • David B. Knaff
Part of the Advances in Photosynthesis and Respiration book series (AIPH, volume 4)

Summary

Ferredoxin, a Mr=11 kDa protein that contains a single low potential [2Fe-2S] cluster, serves as the ultimate acceptor of electrons from Photosystem I. In addition to serving as the electron donor for NADP+ reduction, a reaction catalyzed by the FAD-containing, membrane-associated enzyme ferredoxin: NADP+ oxidoreductase, ferredoxin also serves as the electron donor to a number of soluble enzymes involved in nitrogen metabolism, sulfur metabolism and the regulation of carbon metabolism. This chapter describes the current state of our knowledge of the structure of ferredoxin and of these ferredoxin-dependent enzymes, of the biosynthesis of these proteins and of the mode of interaction between ferredoxin and its electron-accepting, reaction-partner proteins.

Keywords

Nitrite Reductase Sulfite Reductase Anabaena Variabilis Chemical Modification Study Spinach Ferredoxin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Alam J, Whitaker RA, Krogmann DW and Curtis SE (1986) Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120. J Bacteriol 168: 1265–1271PubMedGoogle Scholar
  2. Aliverti A, Jansen T, Zanetti G, Ronchi S, Herrmann RG and Curti B (1990) Expression in Escherichia coli of ferredoxin: NADP+ reductase from spinach. Eur J Biochem 191: 551–555PubMedCrossRefGoogle Scholar
  3. Aliverti A, Lübberstedt T, Zanetti G, Herrmann RG and Curti B (1991) Probing the role of Lys116 and Lys244 in the spinach ferredoxin-NADP+ reductase by site-directed mutagenesis. J Biol Chem 266: 17760–17763PubMedGoogle Scholar
  4. Aliverti A, Piubelli L, Zanetti G, Lübberstedt T, Herrmann RG and Curti B (1993) The role of cysteine residues of spinach ferredoxin-NADP+ reductase as assessed by site-directed mutagenesis. Biochemistry 32: 6374–6380PubMedCrossRefGoogle Scholar
  5. Aliverti A, Hagen WR and Zanetti G (1995) Direct electrochemistry and EPR spectroscopy ofspinach ferredoxin mutants with modified electron transfer properites. FEBS Lett 368: 220–224PubMedCrossRefGoogle Scholar
  6. Aoki H and Ida S (1994) Nucleotide sequence of a rice root ferredoxin-NADP+ reductase cDNA and its induction by nitrate. Biochim Biophys Acta 1183: 553–556PubMedGoogle Scholar
  7. Aoki H, Doyama N and Ida S (1994) Sequence of a cDNA encoding rice leaf ferredoxin-NADP+ reductase. Plant Physiol 104: 1473–1474PubMedCrossRefGoogle Scholar
  8. Aparicio PJ, Knaff DB and Malkin R (1975) The role of an iron-sulfur center and siroheme in spinach nitrite reductase. Arch Biochem Biophys 169: 102–107PubMedCrossRefGoogle Scholar
  9. Aslam M and Huffaker RC (1989) Role of nitrate and nitrite in the induction of nitrite reductase in leaves of barley seedlings. Plant Physiol 91: 1152–1156PubMedGoogle Scholar
  10. Avila C, Márquez AJ, Pajuelo P, Cannell ME, Wallsgrove RM and Forde BG (1993) Cloning and sequence analysis of a cDNA for barley ferredoxin-dependent glutamate synthase and molecular analysis of photorespiratory mutants deficient in the enzyme. Planta 189: 475–83PubMedCrossRefGoogle Scholar
  11. Back E, Burkhardt W, Moyer M, Privalle L and Rothstein S (1988) Isolation of cDNA clones coding for spinach nitrite reductase: Complete sequence and nitrate induction. Mol Gen Genet 212: 20–26PubMedCrossRefGoogle Scholar
  12. Back E. Dunne W, Schneiderbauer A, de Framond A, Rastogi R and Rothstein SJ (1991) Isolation of the spinach nitrite reductase gene promoter which confers nitrate inducibility on GUS gene expression in transgenic tobacco. Plant Mol Biol 17: 9–18PubMedCrossRefGoogle Scholar
  13. Barker WC, George DG, Srinivasarao GY and Yeh LS (1992) Database of protein sequence alignments. Biophys J 61: A348Google Scholar
  14. Batie CJ and Kamin H (1981) The relation of pH and oxidation-reduction potential to the association state of the ferredoxin-ferredoxin: NADP+ reductase complex. J Biol Chem 256: 7756–7763PubMedGoogle Scholar
  15. Batie CJ and Kamin H (1984a) Ferredoxin: NADP+ oxidoreductase. Equilibria in binary and ternary complexes with NADP+ and ferredoxin. J Biol Chem 259: 8832–8839PubMedGoogle Scholar
  16. Batie CJ and Kamin H (1984b) Electron transfer by ferredoxin NADP+ reductase. Rapid-reaction evidence for participation of a ternary complex. J Biol Chem 259: 11976–11985PubMedGoogle Scholar
  17. Batie CJ and Kamin H (1986) Association of ferredoxin-NADP+ reductase with NADP(H). Specificity and oxidation-reduction properties. J Biol Chem 261: 11214–11223PubMedGoogle Scholar
  18. Bayer E, Josef D, Krauss P, Hagenmaier H, Roder A and Trebst A. (1967) Abbau und resynthese des aktifzentrums von pflanzen ferredoxin. Biochim Biophys Acta 143: 435–437PubMedGoogle Scholar
  19. Berzborn RJ, Klein-Hitpass L, Otto J, Schünemann S, Oworah-Nkruma R and Meyer HE (1990) The ‘additional subunit’ NADP+ of the photosynthetic ATP-synthase and the thylakoid polypeptide binding ferredoxin NADP reductase: Are they different? Z Naturforsch 45c: 60–71Google Scholar
  20. Bhattacharyya AK, Meyer TE and Tollin G (1986) Reduction kinetics of the ferredoxin-NADP+ reductase complex: A laser flash photolysis study. Biochemistry 25: 4655–4661CrossRefGoogle Scholar
  21. Böhme H and Haselkorn R (1988) Molecular cloning and nucleotide sequence analysis of the gene coding for heterocyst ferredoxin from the cyanobacterium Anabaena sp. strain PCC 7120. Mol Gen Genet 214: 278–285PubMedGoogle Scholar
  22. Böhme H and Schrautemeier B (1987a) Comparative characterization of ferredoxins from heterocysts and vegetative cells of Anabaena variabilis. Biochim Biophys Acta 891: 1–7Google Scholar
  23. Böhme H and Schrautemeier B (1987b) Electron donation to nitrogenase in a cell-free system from heterocysts of Anabaena variabilis. Biochim Biophys Acta 891: 115–120Google Scholar
  24. Bookjans G, San Pietro A and Böger P (1978) Resolution and reconstitution of spinach ferredoxin-NADP+ reductase. Biochem Biophys Res Comm 80: 759–765PubMedCrossRefGoogle Scholar
  25. Bouges-Bocquet B (1980) Electron and proton transfers from P-430 to ferredoxin-N ADP-reductase in Chlorella cells. Biochim Biophys Acta 590: 223–233PubMedGoogle Scholar
  26. Brandes HK, Larimer FW, Geek MK, Stringer CD, Schürmann P and Hartman FC (1993) Direct identification of the primary nucleophille of thioredoxin f. J Biol Chem 268: 18411–18414PubMedGoogle Scholar
  27. Bruns CM and Karplus PA (1995) Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: Oxidized, reduced and 2’-phospho-S’-AMP bound states. J Mol Biol 247: 125–145PubMedCrossRefGoogle Scholar
  28. Buchanan BB (1991) Regulation of CO2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Arch Biochem Biophys 288: 1–9PubMedCrossRefGoogle Scholar
  29. Cammack R, Rao KK, Bargeron CP, Hutson KG, Andrew PW and Rogers LG (1977) Midpoint redox potentials of plant and algal ferredoxins. Biochem J 168: 205–209PubMedGoogle Scholar
  30. Cammack R, Hucklesby DR and Hewitt EJ (1978) Electron-paramagnetic-resonance studies of the mechanism of leaf nitrite reductase. Biochem J 171: 519–526PubMedGoogle Scholar
  31. Cammack R, Rao KK and Hall DO (1985) Ferredoxins: Structure and function of a ubiquitous group of proteins. Physiol Veg 23: 649–658Google Scholar
  32. Carrillo N and Vallejos RH (1987) Ferredoxin-NADP+ oxidoreductase. In: Barber J (ed) Topics in Photosynthesis, Vol 8, pp 527–560. Elsevier, AmsterdamGoogle Scholar
  33. Carrillo N, Ceccarelli EA, Krapp AR, Boggio S, Ferreyra RG and Viale AM (1992) Assembly of plant ferredoxin-NADP+ oxidoreductase in Escherichia coli requires GroE molecular chaperonins. J Biol Chem 267: 15537–15541PubMedGoogle Scholar
  34. Caspar T and Quail PH (1993) Promoter and leader regions involved in the expression of the Arabidopsis ferredoxin A gene. The Plant J 3: 161–174Google Scholar
  35. Ceccarelli EA, Viale AM, Krapp AR and Carrillo N (1991) Expression, assembly, and processing of an active plant ferredoxin-NADP+ oxidoreductase and its precursor protein in Escherichia coli. J Biol Chem 266: 14283–14287PubMedGoogle Scholar
  36. Chan RL, Carrillo N and Vallejos RH (1985) Isolation and sequencing of an active-site peptide from spinach ferredoxin-NADP+ oxidoreductase after affinity labeling with periodate-oxidized NADP+. Arch Biochem Biophys 240: 172–177PubMedCrossRefGoogle Scholar
  37. Chang CK, Hanson LK, Richardson PF, Young R and Fajer J (1981) π cation radicals of ferrous and free base isobac-teriochlorins: Models for siroheme and sirohydrochlorin. Proc Natl Acad Sci USA 78: 2652–2656PubMedGoogle Scholar
  38. Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Velieux FMD and Hol WGJ (1992) Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochemistry 31: 4959–4964PubMedGoogle Scholar
  39. Chen L. Durley RCE, Mathews FS and Davidson VL (1994) Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin and cytochrome c 551. Science 264: 86–90PubMedGoogle Scholar
  40. Chow L-P, Iwadate H, Yano K, Kamo M, Tsugita A, Gardet-Salvi L, Stritt-Etter A-L and Schümann P (1995) Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe−4S] cluster. Eur J Biochem 231: 149–156PubMedCrossRefGoogle Scholar
  41. Cidaria D, Biondi PA, Zanetti G and Ronchi S (1985) The NADP+-binding site of ferredoxin-NADP reductase. Eur J Biochem 146:295–299PubMedCrossRefGoogle Scholar
  42. Cline K, Werner-Washburne M, Lubben TH and Keegstra K (1985a) Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J Biol Chem 260: 3691–3696PubMedGoogle Scholar
  43. Cline JF, Janick PA, Siegel LM and Hoffman BM (1985b) Electron-nuclear double resonance studies of oxidized Escherichia coli sulfite reductase: 1H, 14N, and 57Fe measurements. Biochemistry 24: 7942–7947PubMedCrossRefGoogle Scholar
  44. Correll CC, Batie CJ, Ballou DP and Ludwig ML (1992) Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe−2S]. Science 258: 1604–1610.PubMedGoogle Scholar
  45. Correll CC, Ludwig ML, Bruns CM and Karplus PA (1993) Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Sci 2: 2112–2133PubMedGoogle Scholar
  46. Day EP, Peterson J, Bonvoisin JJ, Young LJ, Wilkerson JO and Siegel LM (1988) Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S=1/2 states. Biochemistry 27: 2126–2132PubMedGoogle Scholar
  47. de Boer DA and Weisbeek PJ (1991) Chloroplast protein topogenesis: Import, sorting and assembly. Biochim Biophys Acta 1071:221–253Google Scholar
  48. Decottingnies P, Schmitter J-M, Jacquot J-P, Dutka S, Picaud A and Gadal PA (1990) Purification, characterization, and complete amino acid sequence of a thioredoxin from a green alga, Chlamydomonas reinhardtii. Arch Biochem Biophys 280: 112–121Google Scholar
  49. de la Torre A, Lara C, Yee BC, Malkin R and Buchanan BB (1982) Physicochemical properties of ferralterin, a regulatory iron-sulfur protein functional in oxygenic photosynthesis. Arch Biochem Biophys 213: 545–550PubMedGoogle Scholar
  50. De Pascalis AR, Jelesarov I, Ackermann F, Koppenol WH, Hirasawa M, Knaff DB and Bosshard HR (1993) Binding of ferredoxin to ferredoxin: NADP+ oxidoreductase: The role of carboxyl groups, electrostatic surface potential, and molecular dipole moment. Protein Sci 2: 1126–1135PubMedGoogle Scholar
  51. De Pascalis AR, Schümann P and Bosshard HR (1994) Comparison of the binding sites of plant ferredoxin for two ferredoxin-dependent enzymes. FEBS Lett 337: 217–220PubMedGoogle Scholar
  52. Dickey LF, Gallo-Meagher M and Thompson WF (1992) Light regulatory sequences are located within the 5′ portion of the Fed-1 message sequence. EMBO J 11: 2311–2317PubMedGoogle Scholar
  53. Dobres MS, Elliott RC, Watson JC and Thompson WF (1987) A phytochrome regulated pea transcript encodes ferredoxin I. Plant Mol Biol 8: 53–59CrossRefGoogle Scholar
  54. Droux M, Miginiac-Maslow M, Jacquot J-P, Gadal P, Crawford NA, Kosower NS and Buchanan BB (1987a) Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation. Arch Biochem Biophys 256: 372–380PubMedGoogle Scholar
  55. Droux M, Jacquot J-P, Miginac-Maslow M, Gadal P, Huet JC, Crawford NA, Yee BC and Buchanan BB (1987b) Ferredoxin-thioredoxin reductase, an iron-sulfur enzyme linking light to enzyme regulation in oxygenic photosynthesis: Purification and properties of the enzyme from C3, C4, and cyanobacterial species. Arch Biochem Biophys 252: 426–439PubMedCrossRefGoogle Scholar
  56. Dunham WR, Palmer G, Sands RH and Bearden AJ (1971) On the structure of the iron-sulfur complex in the two-iron ferredoxins. Biochim Biophys Acta 253: 373–384PubMedGoogle Scholar
  57. Elliott RC, Pedersen TJ, Fristensky B, White MJ, Dickey LF and Thompson WF (1989a) Characterization of a single copy gene encoding ferredoxin I from pea. The Plant Cell 1: 681–690PubMedGoogle Scholar
  58. Elliott RC, Dickey LF, White MJ and Thompson WF (1989b) cis-Acting elements for light regulation of pea ferredoxin 1 gene expression are located within the transcribed sequences. The Plant Cell 1:691–698PubMedGoogle Scholar
  59. Falkenstein E, Schwaewen AV and Scheibe R (1994) Full-length cDNA sequences for both ferredoxin-thioredoxin reductase subunits from spinach (Spinacia oleracea L.) Biochim Biophys Acta 1185:252–254PubMedGoogle Scholar
  60. Farrington JA, Land EJ and Swallow AJ (1980) The one-electron potentials of NAD. Biochim Biophys Acta 590: 273–276PubMedGoogle Scholar
  61. Florencio FJ, Yee BC, Johnson TC and Buchanan BB (1988) An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch Biochem Biophys 266: 496–507PubMedCrossRefGoogle Scholar
  62. Flügge U-F and Hinz G (1986) Energy dependence of protein transport into chloroplasts. Eur J Biochem 160: 563–570PubMedGoogle Scholar
  63. Friedman AL and Keegstra K (1989) Chloroplast protein import. Quantitative analysis of precursor binding. Plant Physiol 89: 993–999PubMedGoogle Scholar
  64. Friemann A, Brinkmann K and Hachtel W (1992a) Sequence of a cDNA encoding nitrite reductase from the tree Betulapendula and identification of conserved protein regions. Mol Gen Genet 231: 411–416PubMedCrossRefGoogle Scholar
  65. Friemann A. Lange M, Hachtel W and Brinkmann K (1992b) Induction of nitrate assimilatory enzymes in the tree betula pendula. Plant Physiol 90: 1214–1220Google Scholar
  66. Fry IV, Cammack R, Hucklesby DP and Hewitt EJ (1980) Stability of the nitrosylsirohaem complex of plant nitrite reductase, investigated by EPR spectroscopy. FEBS Lett 111: 377–380PubMedCrossRefGoogle Scholar
  67. Fu W, Drozdzewski PM, Davies MD, Sligar SG and Johnson MK (1992a) Resonance Raman and magnetic circular dichroism studies of reduced [2Fe−2S] proteins. J Biol Chem 267:15502–15510PubMedGoogle Scholar
  68. Fu W, O’Handley S, Cunningham RP and Johnson MK (1992b) The role of the iron-sulfur cluster in Escherichia coli endonuclease III. J Biol Chem 267: 16135–16137PubMedGoogle Scholar
  69. Gadda G, Aliverti A, Ronchi S and Zanetti G (1990) Structure-function relationship in spinach in ferredoxin-NADP+ reductase as studied by limited proteolysis. J Biol Chem 265: 11955–11959PubMedGoogle Scholar
  70. Gallo-Meagher M, Sowinski DA, Elliott RC and Thompson WF (1992) Both internal and external regulatory elements control expression of the pea Fed-1 gene in transgenic tobacco seedlings. Plant Cell 4: 389–395PubMedGoogle Scholar
  71. Galván F, Márquez AJ and Vega JM (1984) Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardtii. Planta 162: 180–187Google Scholar
  72. Génovésio-Taverne J-C, Jetzer Y, Sauder U, Hohenester E, Hughet C, Jansonius JN, Gardet-Salvi L and Schümann P (1991) Crystallization and preliminary X-ray diffraction studies of the spinach-chloroplast thioredoxin f. J Mol Biol 222: 459–461PubMedGoogle Scholar
  73. Gisselmann G, Klausmeier P and Schwenn JD (1993) The ferredoxin:sulphite reductase gene from Synechococcus PCC7942. Biochim Biophys Acta 1144: 102–106PubMedGoogle Scholar
  74. Gleason FK and Holmgren A (1988) Thioredoxin and related proteins in procaryotes. FEMS Microbiol Rev 54: 271–298Google Scholar
  75. Gosset G, Merino E, Recillas F, Oliver G, Becerril B and Bolivar F (1989) Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12. Prot Seq Data Anal 2: 9–16Google Scholar
  76. Gotor C, Pajuelo E, Romero LC, Márquez AJ and Vega JM (1990) Immunological studies of ferredoxin-nitrite reductases and ferredoxin-glutamate synthases from photosynthetic organisms. Arch Microbiol 153: 230–234CrossRefGoogle Scholar
  77. Green LS, Yee BC, Buchanan BB, Kamide K, Sanada Y and Wada K (1991) Ferredoxin and ferredoxin-NADP+ reductase from photosynthetic and nonphotosynthetic tissues of tomato. Plant Physiol 96: 1207–1213PubMedGoogle Scholar
  78. Grossman AR, Bartlett SG, Schmidt GW, Mullet JE and Chua N-H (1982) Optimal conditions for post-translational uptake of proteins by isolated chloroplasts. J Biol Chem 257:1558–1563PubMedGoogle Scholar
  79. Gupta SC and Beevers L (1987) Regulation of nitrite reductase. Plant Physiol 83: 750–754PubMedGoogle Scholar
  80. Hartman H, Syvanen M and Buchanan BB (1990) Contrasting evolutionary histories of chloroplast thioredoxins f and m. Mol Biol Evol 7: 247–254PubMedGoogle Scholar
  81. 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: 77–83PubMedGoogle Scholar
  82. Hervás M, Navarro JA and Tollin G (1992) A laser flash spectroscopy study of the kinetics of electron transfer from spinach Photosystem I to spinach and algal ferredoxins. Photochem Photobiol 56: 319–324Google Scholar
  83. Milliard NP, Hirasawa M, Knaff DB and Shaw RW (1991) A reexamination of the properties of spinach nitrite reductase: Protein and siroheme content heterogeneity in purified preparations. Arch Biochem Biophys 291: 195–199Google Scholar
  84. Hirasawa M and Knaff DB (1985) Interaction of ferredoxin-linked nitrite reductase with ferredoxin. Biochim Biophys Acta 830: 173–180Google Scholar
  85. Hirasawa M and Knaff DB (1993) The role of lysine and arginine residues at the ferredoxin-binding site of spinach glutamate synthase. Biochim Biophys Acta 1144: 85–91Google Scholar
  86. Hirasawa M and Tamura G (1984) Flavin and iron-sulfur containing ferredoxin-linked glutamate synthase from spinach leaves. J Biochem 95: 983–994PubMedGoogle Scholar
  87. Hirasawa M, Fukushima K, Tamura G and Knaff DB (1984) Immunochemical characterization of nitrite reductases from spinach leaves, spinach roots and other higher plants. Biochim Biophys Acta 791: 145–154Google Scholar
  88. Hirasawa M, Boyer JM, Gray KA, Davis DJ and Knaff DB (1986) The interaction of ferredoxin with chloroplast ferredoxin-linked enzymes. Biochim Biophys Acta 851: 23–28Google Scholar
  89. Hirasawa M, Shaw RW, Palmer G and Knaff DB (1987) Prosthetic group content and ligand-binding properties of spinach nitrite reductase. J Biol Chem 262: 12428–12433PubMedGoogle Scholar
  90. Hirasawa M, Sung J-D, Malkin R, Zilber A, Droux M and Knaff DB (1988a) Evidence for the presence of a [2Fe−2S] ferredoxin in bean sprouts. Biochim Biophys Acta 934: 169–176PubMedGoogle Scholar
  91. Hirasawa M. Droux M, Gray KA, Boyer JM, Davis DJ, Buchanan BB and Knaff DB (1988b) Ferredoxin-thioredoxin reductase: Properties of its complex with ferredoxin. Biochim Biophys Acta 935: 1–8.Google Scholar
  92. Hirasawa M, Morrow KJ, Chang K-T and Knaff DB (1989) Circular dichroism, binding and immunological studies on the interaction between spinach ferredoxin and glutamate synthase. Biochim Biophys Acta 977: 150–156Google Scholar
  93. Hirasawa M, Chang K-T and Knaff DB (1990) Characterization of a ferredoxin: NADP+ oxidoreductase from a nonphoto-synthetic plant tissue. Arch Biochem Biophys 276: 251–258PubMedCrossRefGoogle Scholar
  94. Hirasawa M, Chang K-T and Knaff DB (1991) The interaction of ferredoxin and glutamate synthase: Cross-linking and immunological studies. Arch Biochem Biophys 286:171–177PubMedCrossRefGoogle Scholar
  95. Hirasawa M, Robertson DE, Ameyibor E, Johnson MK and Knaff DB (1992) Oxidation-reduction properties of the ferredoxin-linked glutamate synthase from spinach leaf. Biochem Biophys Acta 1100: 105–108PubMedGoogle Scholar
  96. Hirasawa M, de Best J and Knaff DB (1993) The effect of lysine and arginine modifying reagents on spinach ferredoxin:nitrite oxidoreductase. Biochim Biophys Acta 1140: 304–312Google Scholar
  97. Hirasawa M, Tollin G, Salamon Z and Knaff DB (1994a) Transient kinetic and oxidation-reduction studies of spinach ferredoxin:nitrite oxidoreductase. Biochim Biophys Acta 1185: 336–345PubMedGoogle Scholar
  98. Hirasawa M, Proske PA and Knaff DB (1994b) The role of tryptophan in the reaction catalyzed by spinach nitrite reductase. Biochim Biophys Acta 1187: 80–88Google Scholar
  99. Hirasawa M, Kleis-San Francisco S, Proske PA and Knaff DB (1995) The effect of N-bromosuccinimide on ferredoxin: NADP+ oxidoreductase. Arch Biochem Biophys 320: 280–288PubMedCrossRefGoogle Scholar
  100. Holden HM, Jacobsen BL, Hurley JK, Tollin G, Oh B-H, Skjeldal L, Chae YK, Cheng H, Xia B and Markley JL (1994) Structure-function studies of [2Fe−2S] ferredoxins. J Bioenerg Biomembr 26: 67–88PubMedCrossRefGoogle Scholar
  101. Huisman JG, Moorman AFM and Verkley FN (1978) In vitro synthesis ofchloroplast ferredoxin as a high molecular weight precursor in a cell-free protein synthesizing system from wheat germ. Biochem Biophys Res Comm 82: 1121–1131PubMedCrossRefGoogle Scholar
  102. Hurley JK, Salamon Z, Meyer TE, Fitch JC, Cusanovich MA, Markley JL, Cheng H, Xia B, Chae YK, Medina M, Gómez-Moreno C and Tollin G (1993a) Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: Site-directed mutagenesis and laser flash photolysis. Biochemistry 32: 9346–9354PubMedCrossRefGoogle Scholar
  103. Hurley JK, Cheng H, Xia B, Markley JL, Medina M, Gómez-Moreno C and Tollin G (1993b) An aromatic amino acid is required at position 65 in Anabaena ferredoxin for rapid electron transfer to ferredoxin: NADP+ reductase. J Am Chem Soc 115: 11698–11701CrossRefGoogle Scholar
  104. Hurley JK, Medina M, Gómez-Moreno C and Tollin G (1994) Further characterization by site-directed mutagenesis of the protein-protein interaction in the ferredoxin/ferredoxin: DAP+ reductase system from Anabaena: Requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer. Arch Biochem Biophys 312: 480–486PubMedCrossRefGoogle Scholar
  105. Ikemizu S, Bando M, Sato T, Morimoto Y, Tsukihara T and Fukuyama K (1994) Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8 Å resolution. Acta Cryst D 50: 167–174CrossRefGoogle Scholar
  106. Iwadate H, Yano K, Aso A, Kamo M, Gardet-Salvi L, Schümann P and Tsugita A (1992) Structure of spinach ferredoxin-thioredoxin reductase. In: Murata N (ed) Research in Photosynthesis, Vol II, pp 539–542. Kluwer, DordrechtGoogle Scholar
  107. Iwadate H, Yano K, Kamo M, Gardet-Salvi L, Schümann P and Tsugita A (1994) Amino acid sequence of the spinach ferredoxin-thioredoxin reductase variable subunit. Eur J Biochem 223: 465–471PubMedCrossRefGoogle Scholar
  108. Jacobson BL, Chae YK, Markley JL, Rayment I and Holden HM (1993) Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-Å resolution. Biochemistry 32: 6788–6793PubMedCrossRefGoogle Scholar
  109. Jalesarov I and Bosshard HR (1994) Thermodynamics of ferredoxin binding to ferredoxin: NADP+ reductase and the role ofwater at the complex interface. Biochemistry 33: 13321–3328.Google Scholar
  110. Jelesarov I, De Pascalis AR, Koppenol WH, Hirasawa M, Knaff DB and Bosshard HR (1993) Ferredoxin binding site on ferredoxin: NADP+ reductase. Differential chemical modification of free and ferredoxin-bound enzyme. Eur J Biochem 216: 57–66PubMedCrossRefGoogle Scholar
  111. Kamo M, Tsugita A, Wiessner C, Wedel N, Bartling D, Herrmann RG, Aguilar F, Gardet-Salvi L and Schümann P (1989) Primary structure of spinach-chloroplast thioredoxin f. Eur J Biochem 182: 315–322PubMedCrossRefGoogle Scholar
  112. Karplus PA (1991) Structure/function of spinach ferredoxin: NADP+ oxidoreductase. In: Müller F (ed) Chemistry and Biochemistry of Flavoproteins, Vol 2, pp 449–455. CRC Press, Boca Raton.Google Scholar
  113. Karplus PA and Bruns CM (1994) Structure-function relations for ferredoxin reductase. J Bioenerg Biomembr 26: 89–99PubMedCrossRefGoogle Scholar
  114. Karplus PA, Daniels MJ and Herriott JR (1991) Atomic structure of ferredoxin-NADP+ reductase: Prototype for a structurally novel flavoenzyme family. Science 251: 60–66PubMedGoogle Scholar
  115. Kassner RJ and Yang W (1977) A theoretical model for the effects of solvent and protein dielectric on the redox properties of iron-sulfur clusters. J Am Chem Soc 99: 4351–4355PubMedCrossRefGoogle Scholar
  116. Katti SK, LeMaster DM and Eklund H (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212: 167–184PubMedCrossRefGoogle Scholar
  117. Kaufman J, Spicer LD and Siegel LM (1993) Proton NMR of Escherichia coli sulfite reductase: The unligated hemeprotein subunit. Biochemistry 32: 2853–2867PubMedGoogle Scholar
  118. Kaufman LS, Roberts LL, Briggs WR and Thompson WF (1986) Phytochrome control of specific mRNA levels in developing pea buds: Kinetics of accumulation, reciprocity, and escape kinetics of the low fluence response. Plant Physiol 81: 1033–1038.CrossRefPubMedGoogle Scholar
  119. Keegstra K and Olsen LJ (1989) Chloroplastic precursors and their transport across the envelope membranes. Ann Rev Plant Physiol 40: 471–501Google Scholar
  120. Kendall AC, Wallsgrove RM, Hall NP, Turner JC and Lea PJ (1986) Carbon and nitrogen metabolism in barley (Hordeum vulgare L.) mutants lacking ferredoxin-dependent glutamate synthase. Planta 168: 316–323CrossRefGoogle Scholar
  121. Kimata Y and Hase T (1989) Localization of ferredoxin isoproteins in mesophyll and bundle sheath cells in maize leaf. Plant Physiol 89: 1193–1197PubMedGoogle Scholar
  122. Knaff DB and Hirasawa M (1991) Ferredoxin-dependent enzymes. Biochim Biophys Acta 1056: 93–125PubMedGoogle Scholar
  123. Knaff DB, Hirasawa M, Ameyibor E, Fu W and Johnson MK (1991) Spectroscopic evidence for a [3Fe-4S] cluster in spinach glutamate synthase. J Biol Chem 266: 15050–15084Google Scholar
  124. Kramer V, Lahners K, Back E, Privalle LS and Rothstein S (1989) Transient accumulation of nitrite reductase mRNA in maize following the addition of nitrite. Plant Physiol 90: 1214–1220PubMedGoogle Scholar
  125. Kronenberger J, Lepingle A, Caboche M and Vaucheret H (1993) Cloning and expression of distinct nitrite reductases in tobacco leaves and roots. Mol Gen Genet 23: 203–208Google Scholar
  126. Krueger RJ and Siegel LM (1982a) Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase. Biochemistry 21: 2892–2904PubMedGoogle Scholar
  127. Krueger RJ and Siegel LM (1982b) Evidence for siroheme-Fe4S4 interaction in spinach ferredoxin-sulfite reductase. Biochemistry 21: 2905–2909PubMedGoogle Scholar
  128. Lahners K, Kramer V, Back E, Privalle L and Rothstein S (1988) Molecular cloning of complementary DNA encoding maize nitrite reductase. Plant Physiol 88: 741–746PubMedGoogle Scholar
  129. Lancaster JR, Vega JM, Kamin H, Orme-Johnson NR, Orme-Johnson WH, Krueger RJ and Siegel LM (1979) Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism. J Biol Chem 254: 1268–1272PubMedGoogle Scholar
  130. Lancelin J-M, Stein M and Jacquot J-P (1993) Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. J Biochem 114: 421–431PubMedGoogle Scholar
  131. Land EJ and Swallow AJ (1968) One-electron reactions in biochemical systems as studied by pulse radiolysis. Biochim Biophys Acta 162: 327–337PubMedGoogle Scholar
  132. Lea PJ, Robinson SA and Stewart GR (1990) The enzymology and metabolism of glutamine, glutamate and asparagine. In: Miflin B J and Lea PJ (eds) The Biochemistry of Plants, Vol 16, pp 121–159. Academic Press, New YorkGoogle Scholar
  133. Li H-M, Theg SM, Bauerle CM and Keegstra K (1990) Metalion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts. Proc Natl Acad Sci USA 87: 6748–6752PubMedGoogle Scholar
  134. Lubben TH, Donaldson GK, Viitanen P and Gatenby AA (1989) Several proteins imported into chloroplasts form stable complexes with groEL related chloroplast molecular chaperone. Plant Cell 1: 1223–1230PubMedCrossRefGoogle Scholar
  135. Luque I, Flores E and Herrero A (1993) Nitrite reductase gene from Synechococcus sp. PCC 7942: Homology between cyanobacterial and higher-plant nitrite reductase. Plant Mol Biol 21: 1201–1205PubMedCrossRefGoogle Scholar
  136. Luque I, Flores E and Herrero A (1994) Nitrate and nitrite transport in the cyanobacterium Synechococcus sp. PCC 7942 are mediated by the same permease. Biochim Biophys Acta 1184: 296–298Google Scholar
  137. Marc-Martin S, Spielmann A, Stutz E and Schümann P (1993) Cloning and sequencing of a corn (Zea mays) nuclear gene coding for the chloroplast specific catalytic subunit of ferredoxin-thioredoxin reductase. Biochim Biophys Acta 1183: 207–209PubMedGoogle Scholar
  138. Marqués S, Florencio FJ and Candau P (1992) Purification and characterization of the ferredoxin-glutamate synthase from the unicellular cyanobacterium Synechococcus sp. PCC 6301. Eur J Biochem 206: 69–77PubMedGoogle Scholar
  139. Márquez AJ, Gotor C, Romero LC, Galván F and Vega JM (1986) Ferredoxin-glutamate synthase from Chlamydomonas reinhardtii. Prosthetic groups and preliminary studies of mechanism. Int J Biochem 18: 531–535Google Scholar
  140. Márquez AJ, Avila C, Forde BG and Wallsgrove RM (1988) Ferredoxin-glutamate synthase from barley leaves: Rapid purification and partial characterization. Plant Physiol Biochem 26: 645–651Google Scholar
  141. Masaki R, Yoshikawa S and Matsubara H (1982) Steady-state kinetics of reduced ferredoxin with ferredoxin-NADP+ reductase. Biochim Biophys Acta 700: 101–109Google Scholar
  142. Matsubara H and Hase T (1983) Phylogenetic consideration of ferredoxin sequences in plants, particularly algae. In: Jensen U and Fairbanks DE (eds) Proteins and Nucleic Acids in Plant Systematics, pp 245–266. Springer-Verlag, BerlinGoogle Scholar
  143. Matsubara H, Hase T, Wakabayahi S and Wada K (1980) Structure and evolution ofchloroplast–and bacterial-type ferredoxin. In: Sigman DS and Brazier HAB (eds) The Evolution of Protein Structure and Function, pp 245–266. Academic Press, New YorkGoogle Scholar
  144. Matthijs HCP, Coughlan SJ and Hind G (1986) Removal of ferredoxin: NADP+ oxidoreductase from the thylakoid membranes, rebinding to depleted membranes, and identification of the binding site. J Biol Chem 261: 12154–12158.PubMedGoogle Scholar
  145. Mayhew SG and Tollin G (1992) General properties of flavodoxin. In: Muller F (ed) Chemistry and Biochemistry of Flavoenzymes, Vol III. pp 389–426. CRC Press, Boca RatonGoogle Scholar
  146. McRee DE, Richardson DC, Richardson JS and Siegel LM (1986) The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase. J Biol Chem 261: 10277–10281PubMedGoogle Scholar
  147. Medina M, Mendez E and Gómez-Moreno C (1992a) Identification of arginyl residues involved in the binding of ferredoxin-NADP+ reductase from Anabaena sp PCC 7119 to its substrates. Arch Biochem Biophys 299: 281–286PubMedCrossRefGoogle Scholar
  148. Medina M, Mendez E and Gómez-Moreno C (1992b) Lysine residues on ferredoxin-NADP+ reductase from Anabaena sp. PCC 7119 involved in substrate binding. FEES Lett 298: 25–28.CrossRefGoogle Scholar
  149. Medina M, Gómez-Moreno C and Tollin G (1992c) Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions. Eur J Biochem 210: 577–583PubMedCrossRefGoogle Scholar
  150. Medina M, Peleato ML, Mendez E and Gómez-Moreno C (1992d) Identification of specific carboxyl groups on Anabaena PCC 7119 flavodoxin which are involved in the interaction with ferredoxin-NADP+ reductase. Eur J Biochem 203: 373–379PubMedCrossRefGoogle Scholar
  151. Medina M, Bazo IG, Fillat MF and Gómez-Moreno C (1993) Structure predictions of ferredoxin-NADP+ reductase from the cyanobacterium Anabaena sp PCC 7119. Prot Seq Data Anal 5: 247–252Google Scholar
  152. Mikami B and Ida S (1989) Spinach ferredoxin-nitrite reductase: Characterization of catalytic activity and interaction of the enzyme with substrates. J Biochem 105: 47–50PubMedGoogle Scholar
  153. Mohr H, Neininger A and Seith B (1992) Control of nitrate reductase and nitrite reductase gene expression by light, nitrite and a plastidic factor. Bot Acta 105: 81–89Google Scholar
  154. Morigasaki S, Takata K, Sanada Y, Wada K, Yee BC, Shin M and Buchanan BB (1990a) Novel forms of ferredoxin and ferredoxin-NADP reductase from spinach roots. Arch Biochem Biophys 283: 75–80PubMedCrossRefGoogle Scholar
  155. Morigasaki S, Takata K, Suzuki T and Wada K (1990b) Purification and characterization of a ferredoxin-NADP+ oxidoreductase-like enzyme form radish root tissues. Plant Physiol 93: 896–901PubMedCrossRefGoogle Scholar
  156. Muller EGD and Buchanan BB (1989) Thioredoxin is essential for photosynthetic growth. J Biol Chem 264: 4008–4014PubMedGoogle Scholar
  157. Nagaoka S, Hirasawa M, Fukushima K and Tamura G (1984) Methyl viologen-linked nitrite reductase from bean roots. Agric Biol Chem 48: 1179–1188Google Scholar
  158. Nakatani S and Shin M (1991) The reconstituted NADP photoreducing system by rebinding of the large form of ferredoxin-NADP reductase to depleted thylakoid membranes. Arch Biochem Biophys 291: 390–394PubMedCrossRefGoogle Scholar
  159. Nalbantoglu B, Hirasawa M, Moomaw C, Nguyen H, Knaff DB and Allen R (1994) Cloning and sequencing of the gene encoding spinach ferredoxin-dependent glutamate synthase. Biochim Biophys Acta 1183: 557–561PubMedGoogle Scholar
  160. Neininger A, Kronenberger J and Mohr H (1992) Coaction of light, nitrate and a plastidic factor in controlling nitrite-reductase gene expression in tobacco. Planta 187: 381–387CrossRefGoogle Scholar
  161. Neininger A, Bichler J, Schneiderbauer A and Mohr H (1993) Response of a nitrite-reductase 3.1-kilobase upstream regulatory sequence from spinach to light and nitrate in transgenic tobacco. Planta 189: 440–442Google Scholar
  162. Neininger A, Seith B, Hoch B and Mohr H (1994a) Gene expression of nitrite reductase in Scots pine (Pinus sylvestris L.) as affected by light and nitrate. Plant Molec Biol 25: 449–457.Google Scholar
  163. Neininger A, Back E, Bichler J, Schneiderbauer A and Mohr H (1994b) Deletion analysis ofa nitrite-reductase promoter from spinach in transgenic tobacco. Planta 194: 186–192Google Scholar
  164. Nozaki Y, Tamaki M and Shin M (1985) The reconstituted NADP+ photoreducing system by recombination of ferredoxin-NADP+ reductase and connectein with thylakoids. Physiol Vèg 23: 627–633Google Scholar
  165. Oelmüller R, Bolle C, Tyagi AK, Niekrawitz N, Breit S and Herrmann RG (1993) Characterization of the promoter from the single-copy gene encoding ferredoxin-NADP+-oxido-reductase from spinach. Mol Gen Genet 237: 261–272PubMedGoogle Scholar
  166. Ogawa M and Ida S (1987) Biosynthesis of ferredoxin-nitrite Sreductase in rice seedlings. Plant Cell Physiol 28: 1501–1508Google Scholar
  167. Olsen LJ, Theg SM, Selman BR and Keegstra K (1989) ATP is required for the binding of precursor proteins to chloroplasts. J Biol Chem 264: 6724–6729PubMedGoogle Scholar
  168. Ondrias MR, Carson SD, Hirasawa M and Knaff DB (1985) Characterization of the siroheme active site in spinach nitrite reductase. Biochim Biophys Acta 830: 159–163PubMedGoogle Scholar
  169. Oralin EG, Calcaterra NB, Carrillo N and Ceccarelli EA (1993) Probing the role of the carboxyl-terminal region of ferredoxin-NADP+ reductase by site-directed mutagenesis and deletion analysis. J Biol Chem 268: 19267–19273Google Scholar
  170. Ostrowski J, Wu J-Y, Rueger DC, Miller BE, Siegel LM and Kredich M (1989) Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. J Biol Chem 264: 15726–15737PubMedGoogle Scholar
  171. Pain D and Blobel G (1987) Protein import into chloroplasts requires a chloroplast ATPase. Proc Natl Acad Sci USA 84: 3288–3292PubMedGoogle Scholar
  172. Pajuelo E, Borrero JA and Marquez AJ (1993) Immunoiogical approach to subunit composition off erredoxin-nitrite reductase from Chlamydomonas reinhardtii. Plant Sci 95: 9–21CrossRefGoogle Scholar
  173. Palmer, G (1973) Current insights into the active center of spinach ferredoxin and other iron-sulfur proteins. In: Lovenberg W (ed) The Iron-Sulfur Proteins, Vol 2, pp 285–325. Academic Press, New YorkGoogle Scholar
  174. Pelanda R, Vanoni MA, Perego M, Piubelli L, Galizzi A, Curti B and Zanetti G (1993) Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing and analysis of functional domains. J Biol Chem 268: 3099–3106PubMedGoogle Scholar
  175. Pelletier H and Kraut J (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258: 1748–1755PubMedGoogle Scholar
  176. Perry SE, Buvinger WE, Bennett J and Keegstra K (1991) Synthetic analogs of a transit peptide inhibit binding or translocation of chloroplast precursor proteins. J Biol Chem 266: 11882–11889PubMedGoogle Scholar
  177. Pilon M, de Boer AD, Knols SL, Koppelman MHGM, van der Graaf RM, de Kruijff B and Weisbeek PJ (1990) Expression in Escherichia coli and purification of a translocation-competent precursor of the chloroplast protein ferredoxin. J Biol Chem 265: 3358–3361PubMedGoogle Scholar
  178. Pilon M, de Kruijff B and Weisbeek PJ (1992a) New insights into the mechanism of the ferredoxin precursor into chloroplasts. J Biol Chem 267: 2548–2556PubMedGoogle Scholar
  179. Pilon M, Weisbeek PJ and de Kruijff B (1992b) Kinetic analysis of translocation into isolated chloroplasts of the purified ferredoxin precursor. FEBS Lett 302: 65–68PubMedCrossRefGoogle Scholar
  180. Porqué PG, Baldesten A and Reichard P (1970) Purification of a thioredoxin system from yeast. J Biol Chem 245: 2363–2370Google Scholar
  181. Privalle LS, Privalle CT, Leonardy NJ and Kamin H (1985) Interactions between spinach ferredoxin-nitrite reductase and its substrates. J Biol Chem 260: 14344–14350PubMedGoogle Scholar
  182. Pueyo JJ and Gómez-Moreno C (1991) Characterization of the cross-linked complex formed between ferredoxin-NADP+ reductase and flavodoxin from Anabaena PCC 7119. Biochim Biophys Acta 1059: 149–156Google Scholar
  183. Pueyo JJ, Gómez-Moreno C and Mayhew SG (1991) Oxidation-reduction potentials of ferredoxin-NADP+ oxidoreductase and flavodoxin from Anabaena PCC 7119 and their electrostatic complexes. Eur J Biochem 202: 1065–1071PubMedCrossRefGoogle Scholar
  184. Pueyo JJ, Revilla C, Mayhew SG and Gómez-Moreno C (1992) Complex formation between ferredoxin and ferredoxin-NADP+ reductase from Anabaena PCC 7119. Arch Biochem Biophys 294: 367–372PubMedCrossRefGoogle Scholar
  185. Rastogi R, Back E, Schneiderbauer A, Bowsher CG, Moffatt B and Rothstein S (1993) A 330 bp region of the spinach nitrite reductase gene promoter directs nitrate-inducible tissue-specific expression in transgenic tobacco. Plant J 4: 317–326CrossRefGoogle Scholar
  186. Rebeille F and Hatch MD (1986) Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems. Arch Biochem Biophys 249: 164–170PubMedGoogle Scholar
  187. Redinbaugh MG and Campbell WH (1993) Glutamine synthetase and ferredoxin-dependent glutamate synthase in the maize (Zea mays) root primary response to nitrate. Plant Physiol 101: 1249–1255PubMedGoogle Scholar
  188. Reith ME, Laudenbach DE and Straus NA (1986) Isolation and nucleotide sequence analysis of the ferredoxin I gene from the cyanobactetium Anacyslisnidulans R2. JBacteriol 168: 1319–1324Google Scholar
  189. Robinson C and Ellis RJ (1984) Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in processing imported precursor peptides. Eur J Biochem 142: 337–342PubMedGoogle Scholar
  190. Rogers LJ (1987) Ferredoxins, flavodoxins and related proteins: Structure function and evolution. In: Fay P and van Baalen C (eds) The Cyanobacteria, pp 35–61. Elsevier, AmsterdamGoogle Scholar
  191. Rogers WJ, Hodges M, Decottignies P, Schmitter J-M, Gadal P and Jacquot J-P (1992) Isolation of a cDNA fragment coding for Chlamydomonas reinhardtii ferredoxin and expression of the recombinant protein in Escherichia coli. FEBS Lett 310: 240–245PubMedCrossRefGoogle Scholar
  192. Romero LC, Gotor C, Márquez AJ, Forde B and Vega JM (1988) Antigenic similarities between ferredoxin-dependent nitrite reductase and glutamate synthase from Chlamydomonas reinhardtii. Biochim Biophys Acta 957: 152–157PubMedGoogle Scholar
  193. Rypniewski WR, Breiter DR, Benning MM, Wesenberg G, Oh B-H, Markley JL, Rayment I and Holden HM (1991) Crystallization and structure determination to 2.5-Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry 30: 4126–4131PubMedCrossRefGoogle Scholar
  194. Sakakibara H, Watanabe M, Hase T and Sugiyama T (1991) Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf. J Biol Chem 266: 2028–2035PubMedGoogle Scholar
  195. Sakakibara H, Kawabata S, Hase T and Sugiyama T (1992) Differential effects of nitrate and light on the expression of glutamine synthetases and ferredoxin-dependent glutamate synthase in maize. Plant Cell Physiol 33: 1193–1198Google Scholar
  196. Sakihama N and Shin M (1987) Evidence from high-pressure liquid chromatography for the existence of two ferredoxins in plants. Arch Biochem Biophys 256: 430–434PubMedCrossRefGoogle Scholar
  197. Salamon Z, Gleason FK and Tollin G (1992) Direct electrochemistry of thioredoxins and glutathione at a lipid bilayermodified electrode. Arch Biochem Biophys 299: 193–198PubMedCrossRefGoogle Scholar
  198. Salamon Z, Tollin G, Hirasawa M, Gardet-Salvi L, Stritt-Etter A-L, Knaff DB and Schümann P (1995) The oxidation-reduction properties of spinach thioredoxins f and m and of ferredoxin: thioredoxin reductase. Biochem Biophys Acta 1230: 114–118PubMedGoogle Scholar
  199. Salmeen I and Palmer G (1972) Contact-shifted NMR of spinach ferredoxin: Additional resonances and partial assignments. Arch Biochem Biophys 150: 767–773PubMedCrossRefGoogle Scholar
  200. Sancho J and Gómez-Moreno C (1991) Interaction of ferredoxin-NADP+ reductase from Anabaena with its substrates. Arch Biochem Biophys 288: 231–238PubMedCrossRefGoogle Scholar
  201. Sancho J, Peleato ML, Gómez-Moreno C and Edmondson DE (1988) Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacterium Anabaena variabilis. Arch Biochem Biophys 260: 200–207PubMedCrossRefGoogle Scholar
  202. Sancho J, Medina M, Gómez-Moreno C (1990) Arginyl groups involved in the binding of Anabaena ferredoxin-NADP+ reductase to NADP+ and to ferredoxin. Eur J Biochem 187: 39–49PubMedCrossRefGoogle Scholar
  203. Sands RH and Dunham WR (1975) Spectroscopic studies on two-iron ferredoxin. Quart Rev Biophys 7: 443–504.Google Scholar
  204. Scherer S, Alps I, Sadowski H and Böger P (1988) Ferredoxin-NADP+ oxidoreductase is the respiratory NADPH dehydrogenase of the cyanobacterium Anabaena variabilis. Arch Biochem Biophys 267: 228–235PubMedCrossRefGoogle Scholar
  205. Schluchter WM and Bryant DA (1992) Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: Cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies of the gene product. Biochemistry 31: 3092–3102PubMedGoogle Scholar
  206. Schmitz S, Schrautemeier B and Böhme H (1993) Evidence from directed mutagenes is that positively charged amino acids are necessary for interaction of nitrogenase with the [2Fe-2S] heterocyst ferredoxin (FdxH) from the cyanobacterium Anabaena sp., PCC7120. Mol Gen Genet 240: 455–460PubMedGoogle Scholar
  207. Schnell DJ, Blobel G and Pain D (1991) Signal peptide analogs derived from two chloroplast precursors interact with the signal recognition system of the chloroplast envelope. J Biol Chem 266: 3335–3342PubMedGoogle Scholar
  208. Schrautemeier B and Böhme H (1985) A distinct ferredoxin for nitrogen fixation isolated from heterocysts of the cyanobacterium Anabaena variabilis. FEBS Lett 184: 304–308CrossRefGoogle Scholar
  209. Schuster C and Mohr H (1990) Appearance of nitrite-reductase mRNA in mustard seedling cotyledons is regulated by phytochrome. Planta 181: 327–334Google Scholar
  210. Seith B, Schuster C and Mohr H (1991) Coaction of light, nitrate and a plastidic factor in controlling nitrite-reductase gene expression in spinach. Planta 184: 74–80CrossRefGoogle Scholar
  211. Serre L, Medina M, Gómez-Moreno C, Fontecilla-Camps JC and Frey M (1991) Crystals of Anabaena 7119 ferredoxin-NADP+ reductase. J Mol Biol 218: 271–272PubMedCrossRefGoogle Scholar
  212. Serre L, Vellieux F, Fontecilla-Camps J, Frey M, Medina M and Gómez-Moreno C (1994) Structural study of ferredoxin-NADP+ reductase from Anabaena PCC 7119 and its complex with NADP+ In: Yagi K (ed) Flavins and Flavoproteins 1993, pp 431–434. Walter de Gruyter, BerlinGoogle Scholar
  213. Shin M, Ishida H and Nozaki Y (1985) A new protein factor, connectein, as a constituent of the large form of ferredoxin-NADP reductase. Plant Cell Physiol 26: 559–563Google Scholar
  214. Siegel LM, Rueger DC, Barber MJ, Krueger RJ, Orme-Johnson NR and Orme-Johnson WH (1982) Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters and ligand complexes. J Biol Chem 257: 6343–6350PubMedGoogle Scholar
  215. Skjeldal L, Westler WM, Oh B-H, Krezel AM, Holden HM, Jacobson BL, Rayment I and Markley JL (1991) Two-dimensional magnetization exchange spectroscopy of Anabaena 7120 ferredoxin. Nuclear Overhauser effect and electron-self exchange cross peaks from amino acid residues surrounding the 2Fe–2S* cluster. Biochemistry 30: 7363–7368PubMedGoogle Scholar
  216. Small IS and Gray JC (1984) Synthesis of wheat leaf nitrite reductase de novo following induction with nitrate and light. Eur J Biochem 145: 291–297PubMedCrossRefGoogle Scholar
  217. Smeekens S, van Binsbergen J and Weisbeek P (1985) The plant ferredoxin precursor: Nucleotide sequence of a full length cDNA clone. Nucleic Acids Res 13: 3179–3194PubMedGoogle Scholar
  218. Smeekens S, Bauerle C, Hageman J, Keegstra K and Weisbeek P (1986) The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell 46: 365–375PubMedCrossRefGoogle Scholar
  219. Smeekens S, van Steeg H, Bauerle C, Bettenbroek H, Keegstra K and Weisbeek P (1987) Import into chloroplasts of a yeast mitochondrial protein directed by ferredoxin and plastocyanin transit sequences. Plant Mol Biol 9: 377–388CrossRefGoogle Scholar
  220. Smith JM. Smith WH and Knaff DB (1981) Electrochemical titrations of a ferredoxin-ferredoxin: NADP+ oxidoreductase complex. Biochim Biophys Acta 635: 405–411PubMedGoogle Scholar
  221. Somers DE, Caspar T and Quail PH (1990) Isolation and characterization of a ferredoxin gene from Arabidopsis thaliana. Plant Physiol 93: 572–577PubMedGoogle Scholar
  222. Somerville CR and Ogren WL (1980) Inhibition of photosynthesis in mutants of Arabidopsis lacking glutamate synthase activity. Nature 286: 257–259CrossRefGoogle Scholar
  223. Soncini FC and Vallejos RH (1989) The chloroplast reductase-binding protein is identical to the 16.5 kDa polypeptide described as a component of the oxygen-evolving complex. J Biol Chem 264: 21112–21115PubMedGoogle Scholar
  224. Spano AJ and Schiff JA (1987) Purification, properties and cellular location of Euglena ferredoxin-NADP reductase. Biochim Biophys Acta 894: 484–498PubMedGoogle Scholar
  225. Suzuki A and Gadal P (1982) Glutamate synthase from rice leaves. Plant Physiol 69: 848–852PubMedGoogle Scholar
  226. 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. Plant Physiol 78: 374–378PubMedCrossRefGoogle Scholar
  227. Suzuki I, Sugiyama T and Omata T (1993) Primary structure and transcriptional regulation of the gene for nitrite reductase from the cyanobacterium Synechococcus PCC 7942. Plant Cell Physiol 348: 1311–1320Google Scholar
  228. Suzuki S, Izumihara K and Hase T (1991) Plastid import and iron-sulfur cluster assembly of photosynthetic and nonphotosynthetic ferredoxin isoproteins in maize. Plant Physiol 97: 375–380PubMedGoogle Scholar
  229. Takahashi Y, Hase T, Wada K and Matsubara H (1983) Ferredoxins in developing spinach cotyledons: The presence of two molecular species. Plant Cell Physiol 24: 189–198Google Scholar
  230. Takahashi Y, Mitsui A, Hase T and Matsubara H (1986) Formation of iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proc Natl Acad Sci USA 83: 2434–2437PubMedGoogle Scholar
  231. Takahashi Y, Mitsui A and Matsubara H (1990a) Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts. Plant Physiol 95: 97–103Google Scholar
  232. Takahashi Y, Mitsui A, Fujita Y and Matsubara H (1990b) Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin. Plant Physiol 95: 104–110Google Scholar
  233. Theg SM, Bauerle C, Olsen LJ, Selman BR and Keegstra K (1989) Internal ATP is the only energy source required for the translocation of precursor proteins across chloroplastic membranes. J Biol Chem 264: 6730–6736PubMedGoogle Scholar
  234. Tsugita A, Maeda K and Schumann P (1983) Spinach chloroplast thioredoxins in evolutionary drift. Biochem Biophys Res Comm 115: 1–7PubMedCrossRefGoogle Scholar
  235. Tsukihara T, Fukuyama K, Nakamura M, Katsube Y, Tanaka N, Kakudo M, Wada K, Hase T and Matsubara H (1981) X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 Å resolution. J Biochem 90: 1763–1773Google Scholar
  236. Tsukihara T, Fukuyama K, Mizushima M, Harioka T, Kusunoki M, Katsube Y, Hase T and Matsubara H (1990) Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 Å resolution. J Mol Biol 216: 399–410PubMedGoogle Scholar
  237. Valentin K, Kostrzewa M and Zetsche K (1993) Glutamate synthase is plastid-encoded in a red alga: Implications for the evolution of glutamate synthases. Plant Mol Biol 23: 77–85PubMedCrossRefGoogle Scholar
  238. Vallejos RH, Ceccarelli E and Chan R (1984) Evidence for the existence of a thylakoid intrinsic protein that binds ferredoxin-NADP+ oxidoreductase. J Biol Chem 259: 8048–8051PubMedGoogle Scholar
  239. van der Plas J, de Groot RP, Weisbeek PJ and van Arkel GA (1986a) Coding sequence of a ferredoxin gene from Anabaena variabilis ATCC 29413. Nucleic Acids Res 14: 7803PubMedGoogle Scholar
  240. van der Plas J, de Groot RP, Woortman MR, Weisbeek PJ and van Arkel GA (1986b) Coding sequence of a ferredoxin from Anacystis nidulans R2 (Synechococcus PCC 7942) Nucleic Acids Res 14: 7804PubMedGoogle Scholar
  241. Vanoni MA, Edmondson DE, Zanetti G and Curti B (1992) Characterization of the flavins and iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism and electron paramagnetic resonance spectroscopies. Biochemistry 31: 4613–4623PubMedCrossRefGoogle Scholar
  242. Vega JM and Kamin H (1977) Spinach nitrite reductase. Purification and properties of a siroheme-containing enzyme. J Biol Chem 252: 896–909PubMedGoogle Scholar
  243. Vieira B J, Colvert KK and Davis DJ (1986) Chemical modification and cross-linking as probes of regions on ferredoxin involved in the interaction with ferredoxin: NADP reductase. Biochim Biophys Acta 851: 109–122PubMedGoogle Scholar
  244. Vigara AJ, Bes MT, Vega JM and Gómez-Moreno C (1994) Purification of Fd-glutamate synthase from Monoraphidum braunii and characterization ofa light-dependent activity assay. J Mol Catal 89: 257–266Google Scholar
  245. Vorst O, van Dam F, Oosterhoff-Teertstra R, Smeekens S and Weissbeek P (1990) Tissue-specific expression directed by an Arabidopsis thaliana pre-ferredoxin promoter in transgenic tobacco plants. Plant Mol Biol 14: 491–499PubMedCrossRefGoogle Scholar
  246. Vorst O, van Dam F, Weisbeek P and Smeekens S (1993) Light-regulated expression of the Arabidopsis thaliana ferredoxinA gene involves both transcriptional and post-transcriptional processes. Plant J 3: 793–803PubMedCrossRefGoogle Scholar
  247. Wada K, Oh-Oka H and Matsubara H (1985) Ferredoxin isoproteins and their variation during growth of higher plants. Physiol Vèg 23: 679–686Google Scholar
  248. Wada K, Onda M and Matsubara H (1989) Amino acid sequences of ferredoxin isoproteins from radish roots. J Biochem 105: 619–625PubMedGoogle Scholar
  249. Wagner R, Carrillo N, Junge W and Vallejos RH (1982) On the conformation of reconstituted ferredoxin-NADP+ oxidoreductase in the thylakoid membrane. Biochim Biophys Acta 680: 317–330Google Scholar
  250. Walker MC, Pueyo JJ, Navarro JA, Gómez-Moreno C and Tollin G (1991) Laser flash photolysis studies of the kinetics of reduction of ferredoxins and ferredoxin-NADP+ reductases from Anabaena PCC 7119 and spinach: Electrostatic effects on intracomplex electron transfer. Arch Biochem. Biophys 287: 351–358PubMedCrossRefGoogle Scholar
  251. Wallsgrove RM, Turner JC, Hall NP, Kendall AC and Bright SWJ (1987) Barley mutants lacking chloroplast glutamine synthetase. Biochemical and genetic analysis. Plant Physiol 83: 155–158PubMedGoogle Scholar
  252. Wedel N, Bartling D and Herrmann RG (1988) Analysis of cDNA clones encoding the entire ferredoxin I precursor polypeptide from spinach. Botanica Acta 101: 295–300Google Scholar
  253. Wilkerson JO, Janick PA and Siegel LM (1983) Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and tetranuclear iron-sulfur center prosthetic groups in spinach ferredoxin-nitrite reductase. Biochemistry 22: 5048–5054CrossRefGoogle Scholar
  254. Young LJ and Siegel LM (1988) Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 27: 5984–5990PubMedGoogle Scholar
  255. Zanetti G and Aliverti A (1991) Ferredoxin: NADP+ oxidoreductase. In: Müller F (ed) Chemistry and Biochemistry of Flavoproteins, Vol 2, pp 305–315. CRC Press, Boca RatonGoogle Scholar
  256. Zanetti G and Merati G (1987) Interaction between photosystem I and ferredoxin. Eur J Biochem 169: 143–146PubMedCrossRefGoogle Scholar
  257. Zanetti G, Cidaria D and Curti B (1982) Preparation of apoprotein from spinach ferredoxin-NADP+ reductase. Eur J Biochem 126: 45–458CrossRefGoogle Scholar
  258. Zanetti G, Massey V and Curti B (1983) FAD analogs as mechanistic and ‘domain-binding’ probes of spinach ferredoxin-NAP+ reductase. Eur J Biochem 132: 201–205PubMedCrossRefGoogle Scholar
  259. Zanetti G, Morelli D, Ronchi S, Negri A, Aliverti A and Curti B (1988) Structural studies on the interaction between ferredoxin and ferredoxin-NADP+ reductase. Biochemistry 27: 3753–3759CrossRefGoogle Scholar
  260. Zehnacker C, Becker T W, Suzuki A, Carrayol E, Caboche M and Hirel B (1992) Purification and properties of tobacco ferredoxin-dependent glutamate synthase, and isolation of corresponding cDNA clones. Planta 187: 266–274CrossRefGoogle Scholar
  261. Zilber AL and Malkin R (1988) Ferredoxin cross-links to a 22 kD subunit of Photosystem I. Plant Physiol 88: 810–814PubMedCrossRefGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • David B. Knaff
    • 1
    • 2
  1. 1.Department of Chemistry and BiochemistryTexas Tech UniversityLubbockUSA
  2. 2.Institute for BiotechnologyTexas Tech UniversityLubbockUSA

Personalised recommendations