The chemistry and function of ferredoxin

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References

  1. Akagi, J. M.: The participation of a ferredoxin of Clostridium nigrificans in sulfite reduction. Biochem. Biophys. Res. Commun. 21, 72–77 (1965).

    Article  CAS  Google Scholar 

  2. Aleman, V., S. T. Smith, K. V. Rajagopalan and P. Handler: Soluble metalloflavoproteins. In Non-Heme Iron Proteins: Role in Energy Conversion, A San Pietro, ed. Antioch Press, Yellow Springs, Ohio, pp. 327–348 (1965).

    Google Scholar 

  3. Andrews, I. G. and J. G. Morris: The biosynthesis of alanine by Clostridium kluyveri. Biochim. Biophys. Acta 97, 176–179 (1965).

    Google Scholar 

  4. Apella, E., and A. San Pietro: Physical properties of photosynthetic pyridine nucleotide reductase. Biochem. Biophys. Res. Commun. 6, 349–358 (1962).

    Article  Google Scholar 

  5. Arnon, D. I.: Photosynthetic electron transport and phosphorylation in chloroplasts. In Photosynthesis Mechanisms in Green Plants, Publ. 1145, Nat. Acad. Sci.-Nat. Res. Council (U. S.), pp. 195–212 (1963).

    Google Scholar 

  6. -: Ferredoxin and photosynthesis. Science 149, 1460–1469 (1965).

    Article  CAS  Google Scholar 

  7. — Cell-free photosynthesis and the energy conversion process. In Light and Life, W. D. McElroy and B. Glass, eds. The Johns Hopkins Press, Baltimore, pp. 489–566 (1961).

    Google Scholar 

  8. —, H. Y. Tsujimoto, and B. D. McSwain: Role of ferredoxin in photosynthetic production of oxygen and phosphorylation by chloroplasts. Proc. Natl. Acad. Sci. (U.S.), 51, 1274–1282 (1964).

    Article  CAS  Google Scholar 

  9. —: Photosynthetic phosphorylation and electron transport. Nature 207, 1367–1372 (1965).

    Article  CAS  Google Scholar 

  10. —, F. R. Whatley, and M. B. Allen: Triphosphopyridine nucleotide as a catalyst of photosynthetic phosphorylation. Nature 180, 182–185 (1957).

    Article  CAS  Google Scholar 

  11. —: Assimilatory power in photosynthesis. Science 127, 1026–1034 (1958).

    Article  CAS  Google Scholar 

  12. Bachofen, R., and D. I. Arnon: Crystalline ferredoxin from the photosynthetic bacterium, Chromatium. Biochim. Biophys. Acta, 120, 259 (1966).

    Article  CAS  Google Scholar 

  13. —, B. B. Buchanan, and D. I. Arnon: Ferredoxin as a reductant in pyruvate synthesis by a bacterial extract. Proc. Natl. Acad. Sci. (U. S.) 51, 690–694 (1964).

    Article  Google Scholar 

  14. Barker, H. A.: Bacterial Fermentations, Wiley and Sons, New York 1956.

    Google Scholar 

  15. Bartsch, R. G.: Nonheme iron proteins and Chromatium iron protein. In Bacterial Photosynthesis, H. Gest, A. San Pietro, and L. P. Vernon, eds., Antioch Press, Yellow Springs, Ohio, pp. 315–326 (1963).

    Google Scholar 

  16. Bayer, E., W. Parr, and B. Kazmaier: Aufbau des ferredoxins, des wirkstoffes, der assimilations vorgänge. Arch. Pharmazie 298, 196–206 (1965).

    Article  CAS  Google Scholar 

  17. Bearden, A. J., T. H. Moss, R. G. Bartsch, and M. A. Cusanovitch: Mössbauer spectroscopy studies of Chromatium non-heme iron proteins. In Non-heme Iron Proteins: Role in Energy Conversion A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 87–99 (1965).

    Google Scholar 

  18. Beinert, H.: EPR spectroscopy in the detection, study and identification of protein-bound non-heme iron. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 23–42 (1965).

    Google Scholar 

  19. — , and G. Palmer: Contributions of EPR spectroscopy to our knowledge of oxidative enzymes. Advan. Enzymol. 27, 105–198 (1965).

    CAS  Google Scholar 

  20. Bendall, D. S., R. P. F. Gregory, and R. Hill: Chloroplast ferredoxin from parsley. Biochem. J. 88, 29P–30P (1963).

    Google Scholar 

  21. Bennett, R. and R. C. Fuller: The pyruvate phosphoclastic reaction in Chromatium, a probable role for ferredoxin in a photosynthetic bacterium. Biochem. Biophys. Res. Commun. 16, 300–307 (1964).

    Article  CAS  Google Scholar 

  22. —, N. Rigopoulos, and R. C. Fuller: The pyruvate phosphoclastic reaction and light-dependent nitrogen fixation in bacterial photosynthesis. Proc. Nat. Acad. Sci. (U. S.) 52, 762–768 (1964).

    Article  CAS  Google Scholar 

  23. Blomstrom, D. C., E. Knight, Jr., W. D. Phillips, and J. F. Weiher: The nature of iron in ferredoxin. Proc. Nat. Acad. Sci. (U. S.) 51, 1085–1092 (1964).

    Article  CAS  Google Scholar 

  24. Boyer, P. D.: Spectrophotometric study of the reaction of protein sulfhydryl groups with organic mercurials. J. Am. Chem. Soc. 76, 4331–4337 (1954).

    Article  CAS  Google Scholar 

  25. Bradshaw, W. H., and H. A. Barker: Purification and properties of xanthine dehydrogenase from Clostridium cylindrosporum. J. Biol. Chem. 235, 3620–3629 (1960).

    CAS  Google Scholar 

  26. Bradshaw, W. H., and D. J. Reeder: Ferredoxin coupling to formate oxidation to urate reduction in extracts of Clostridium cylindrosporum. Bacteriol. Proc., p. 110 (1964).

    Google Scholar 

  27. Breslow, R.: On the mechanism of thiamine action. IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80, 3719–3726 (1958).

    Article  CAS  Google Scholar 

  28. Brill, W. J. and R. S. Wolfe: Ferredoxin reduction by acetaldehyde. Fed. Proceed. 24, 233 (1965).

    Google Scholar 

  29. Buchanan, B. B., R. Bachofen, and D. I. Arnon: Role of ferredoxin in the reductive assimilation of CO2 and acetate by extracts of the photosynthetic bacterium Chromatium. Proc. Natl. Acad. Sci. (U. S.) 52, 839–847 (1964).

    Article  CAS  Google Scholar 

  30. — , and M. C. W. Evans: The synthesis of α-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium. Proc. Natl. Acad. Sci. (U. S.) 54, 1212–1218 (1965).

    Article  CAS  Google Scholar 

  31. —, M. C. W. Evans, and D. I. Arnon: Ferredoxin dependent pyruvate synthesis by enzymes of photosynthetic bacteria. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 175–188 (1965).

    Google Scholar 

  32. —, W. Lovenberg, and J. C. Rabinowitz: A comparison of clostridial ferredoxins. Proc. Natl. Acad. Sci. (U. S.) 49, 345–353 (1963).

    Article  CAS  Google Scholar 

  33. — , and J. C. Rabinowitz: Some properties of Methanobacterium omelianskil ferredoxin. J. Bacteriol. 88, 806–807 (1964).

    CAS  Google Scholar 

  34. Cutinelli, C., G. Ehrensvärd, L. Reio, E. Saluste, and R. Stjernholm: Acetic acid metabolism in Rhodospirillum rubrum under anaerobic conditions. Arkiv Kemi 3, 315–322 (1951).

    CAS  Google Scholar 

  35. Davenport, H. E.: Coenzyme reduction by illuminated chloroplasts. Biochem. J. 73, 45P (1959).

    Google Scholar 

  36. -: A protein from leaves catalyzing the reduction of metmyoglobin and triphosphopyridine nucleotide by illuminated chloroplasts. Biochem. J. 77, 471–477 (1960).

    CAS  Google Scholar 

  37. -: The role of soluble protein factor in chloroplast electron transport. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 115–136 (1965).

    Google Scholar 

  38. — , and R. Hill: A protein from leaves catalyzing the reduction of haem-protein compounds by illuminated chloroplasts. Biochem. J. 74, 493–501 (1960).

    CAS  Google Scholar 

  39. —, R. Hill, and F. R. Whatley: A natural factor catalyzing reduction of methaemoglobin by isolated chloroplasts. Proc. Roy. Soc., B., 139, 346–358 (1952).

    Article  CAS  Google Scholar 

  40. D’Eustachio, A. J., and R. W. F. Hardy: Reductants and electron transport in nitrogen fixation. Biochem. Biophys. Res. Commun. 15, 319–323 (1964).

    Article  CAS  Google Scholar 

  41. Evans, M. C. W. and B. B. Buchanan: Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. (U. S.) 53, 1420–1425 (1965).

    Article  CAS  Google Scholar 

  42. — , and D. I. Arnon: A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc. Natl. Acad. Sci. (US) 55, 928–934 (1966).

    Article  CAS  Google Scholar 

  43. Fisher, E.: Bildung von methylenblau als reaktion auf schwefelwasserstoff. Chem. Ber. 16, 2234–2236 (1883).

    Article  Google Scholar 

  44. Fogo, J. K., and M. Popowsky: Spectrophotometric determination of hydrogen sulfide, methylene blue method. Anal. Chem. 21, 732–734 (1949).

    Article  CAS  Google Scholar 

  45. Fredericks, W. W. and E. R. Stadiman: The role of ferredoxin in the hydrogenase system from Clostridium kluyveri. J. Biol. Chem. 240, 4065–4071 (1965).

    Google Scholar 

  46. Fry, K. T., R. A. Lazzarini, and A. San Pietro: The photoreduction of iron in photosynthetic pyridine nucleotide reductase. Proc. Natl. Acid. Sci. (U. S.) 50, 652–657 (1963).

    Article  CAS  Google Scholar 

  47. — , and A. San Pietro: Studies on photosynthetic pyridine nucleotide reductase. Biochem. Biophys. Res. Commun. 9, 218–221 (1962).

    Article  CAS  Google Scholar 

  48. Fry K. T. and A. San Pietro: Photosynthetic pyridine nucleotide reductase. IV. Further studies on the chemical properties of the protein. In Photosynthesis Mechanisms in Green Plants, Publ. 1145, Nat. Acad. Sci.-Nat. Res. Council (U. S.), pp. 252–26 (1963).

    Google Scholar 

  49. Gewitz, H. S., and W. Volker: Über die atmungsfermente der Chlorella. Hoppe-Seyler Z. Physiol. Chem. 330, 124–131 (1962).

    CAS  Google Scholar 

  50. Guillard, R. D., E. D. McKenzie, R. Mason, S. G. Mayhew, J. L. Peel, and J. E. Strangroom: Nature of the non-haem iron in ferredoxin ε rubredoxin. Nature 208, 769–771 (1965).

    Article  Google Scholar 

  51. Gunsalus, I. C.: The chemistry and function of the pyruvate oxidation factor (lipoic acid). J. Cellular Comp. Physiol. 41, Suppl. 1, 113–136 (1953).

    Article  CAS  Google Scholar 

  52. Hall, D. O., T. F. Gibson, and F. R. Whatley: Electron spin resonance spectra of spinach ferredoxin. Biochem. Biophys. Res. Commun. 23, 81–84 (1966).

    Article  CAS  Google Scholar 

  53. Hardy, R. W. F. E. Knight, Jr., C. C. McDonald, and A. J. D’Eustachio: Paramagnetic protein from nitrogen-fixing extracts of Clostridium pasteurianum. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 275–282 (1965).

    Google Scholar 

  54. Hill, R., and F. Bendall: Crystallization of a photosynthetic reductasc from a green plant. Nature 187, 417 (1960).

    Article  CAS  Google Scholar 

  55. — , and A. San Pietro: Hydrogen transport with chloroplasts. Z. Naturforsch. B18, 677–682 (1963).

    Google Scholar 

  56. Hinkson, J. W.: Nicotinamide adenine dinucleotide photoreduction with Chromatium and Rhodospirillum rubrum chromatophores. Arch. Biochem. Biophys. 112, 478–487 (1965).

    Article  CAS  Google Scholar 

  57. Holzer, H., and K. Beaucamp: Nachweis und Charakterisierung von α-lactylthiaminpyrophosphat (“aktives pyruvat”) und α-hydroxyäthyl-thiaminpyrophosphat (“aktiver acetaldehyd”) als Zwischenprodukte der decarboxylierung von pyruvat mit pyruvat decarboxylase aus Bierhefe. Biochim. Biophys. Acta 46, 225–243 (1961).

    Article  CAS  Google Scholar 

  58. Hood, S. L.: Photoreduction of nicotinamide adenine dinucleotide by a cell-free system from Chromatium. Biochim. Biophys. Acta 88, 461–465 (1964).

    CAS  Google Scholar 

  59. Horio, T., and A. San Pietro: Action spectrum for ferricyanide photoreduction and redox potential of chlorophyll 683. Proc. Natl. Acad. Sci. (U. S.) 51, 1226–1231 (1964).

    Article  CAS  Google Scholar 

  60. — , and T. Yamashita: Some properties of photosynthetic pyridine nucleotide reductase from spinach. Biochem. Biophys. Res. Commun. 9, 142–145 (1962).

    Article  CAS  Google Scholar 

  61. Hüidt, A., G. Johansen, K. Linderstrom-Lang, and F. Vaslos: Exchange of deuterium and 18O between water and other substances. 1. Methods Compt. rend. trav. lab. Carlsberg, Ser. chim. 29, 129–157 (1954).

    Google Scholar 

  62. Kimura, T., and K. Suzuki: Enzymatic reduction of non-heme iron protein (adrenodoxin) by reduced nicotinamide adenine dinucleotide phosphate. Biochem. Biophys. Res. Commun. 20, 373–379 (1965).

    Article  CAS  Google Scholar 

  63. Koepsell, H. J., and M. J. Johnson: Dissimilation of pyruvic acid by cell-free preparations of Clostridium butyricum. J. Biol. Chem. 145, 379–386 (1942).

    CAS  Google Scholar 

  64. Lipmann, F.: An analysis of the pyruvic acid oxidation system. Cold Spring Harbor Symposium Quant. Biol. 7, 248–259 (1939).

    CAS  Google Scholar 

  65. Losada, M., and D. I. Arnon: Enzyme systems in photosynthesis. In Modern Methods of Plant Analysis, Vol. VII, H. F. Linskens, B. D. Sanwal, and M. V. Tracey, eds., Springer-Verlag, Berlin, pp. 569–615 (1964).

    Google Scholar 

  66. —, F. R. Whatley, and D. I. Arnon: Separation of two light reactions in noncyclic photophosphorylation of green plants. Nature 190, 606–610 (1961).

    Article  CAS  Google Scholar 

  67. Lovenberg, W., B. B. Buchanan, and J. C. Rabinowitz: Studies on the chemical nature of clostridial ferredoxin. J. Biol. Chem. 238, 3899–3913 (1963).

    CAS  Google Scholar 

  68. Lovenberg, W., M. A. Raftery, and R. D. Cole: Studies on the structure of clostridial ferredoxins. Abstracts of the 148th Meeting of the American Chem. Soc., Chicago, Ill. 22C (1964).

    Google Scholar 

  69. — , and B. E. Sobel: Rubredoxin: A new electron transfer protein from Clostridium pasteurianum. Proc. Natl. Acad. Sci. (U. S.) 54, 193–199 (1965).

    Article  CAS  Google Scholar 

  70. Malkin, R., and J. C. Rabinowitz: Additional observations on the chemistry of clostridial ferredoxin. Biochemistry 5, 1262–1268 (1966).

    Article  CAS  Google Scholar 

  71. Malstrom, B. G. and J. B. Neilands: Metalloproteins. Ann. Rev. Biochem. 33, 331–354 (1964).

    Article  Google Scholar 

  72. Massey, V.: Studies on succinic dehydrogenase. VII. Valency state of the iron in beef heart succinic dehydrogenase. J. Biol. Chem. 229, 763–770 (1957).

    CAS  Google Scholar 

  73. Matsubara, H.: Personal communication (1966).

    Google Scholar 

  74. Mortenson, L. E.: Inorganic nitrogen assimilation and ammonia incorporation. In The Bacteria, III. R. Y. Stanier and I. C. Gunsalus, eds., Academic Press, New York, pp. 119–166 (1962).

    Google Scholar 

  75. -: Nitrogen fixation: Role of ferredoxin in anaerobic metabolism. Ann. Rev. Microbiol. 17, 115–138 (1963).

    Article  CAS  Google Scholar 

  76. -: Ferredoxin requirement for nitrogen fixation by extracts of Clostridium pasteurianum. Biochim. Biophys. Acta. 81, 473–478 (1964).

    CAS  Google Scholar 

  77. -: Ferredoxin and ATP, requirements for nitrogen fixation in cell-free extracts of Clostridium pasteurianum. Proc. Natl. Acad. Sci. (U. S.) 52, 272–279 (1964b).

    Article  CAS  Google Scholar 

  78. -: Purification and analysis of ferredoxin from Clostridium pasteurianum. Biochim. Biophys. Acta 81, 71–77 (1964c).

    CAS  Google Scholar 

  79. -: Nitrogen fixation in extracts of Clostridium pasteurianum. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 243–260 (1965).

    Google Scholar 

  80. —, R. C. Valentine, and J. E. Carnahan: An electron transport factor from Clostridium pasteurianum. Biochem. Biophys. Res. Commun. 7, 448–452 (1962).

    Article  CAS  Google Scholar 

  81. Mortlock, R. P., R. C. Valentine, and R. S. Wolfe: Carbon dioxide activation in the pyruvate clastic system of Clostridium butyricum. J. Biol. Chem. 234, 1653–1656 (1959).

    CAS  Google Scholar 

  82. Omura, T., E. Sanders, D. Y. Cooper, O. Rosenthal, and R. W. Estrabrook: Isolation of a non-heme iron protein of adrenal cortex functional as a TPNH-flavoprotein-cytochrome P450 reductase for hydroxylation reactions. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 401–412 (1965).

    Google Scholar 

  83. Palmer, G. and R. H. Sands: On the magnetic resonance of spinach ferredoxin. J. Biol. Chem. 241, 253 (1966).

    CAS  Google Scholar 

  84. Palmer, G., R. H. Sands, and L. E. Mortenson: Electron paramagnetic resonance studies on the ferredoxin from Clostridium pasteurianum. Biochem. Biophys. Res. Commun. 23, 357–362 (1966).

    Article  CAS  Google Scholar 

  85. Paneque, A., F. F. del Campo, and M. Losada: Nitrite reduction by isolated chloroplasts in light. Nature 198, 90–91 (1963).

    Article  CAS  Google Scholar 

  86. —, J. M. Ramirez, F. F. del Campo, and M. Losada: Light and dark reduction of nitrite in a reconstituted enzymic system. J. Biol. Chem. 239, 1737–1741 (1964).

    CAS  Google Scholar 

  87. Phillips, W. D., E. Knight, Jr., and D. C. Blomstrom: Fe57 Mössbauer spectroscopy and some biological applications. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 69–85 (1965).

    Google Scholar 

  88. Photosynthesis Mechanisms of Green Plants. Publ. 1145. Nat. Acad. Sci.-Nat. Res. Council (U. S.) (1963).

    Google Scholar 

  89. Reaburn, S. and J. C. Rabinowitz: Pyruvate synthesis by a partially purified enzyme from Clostridium acidi-urici. Biochem. Biophys. Res. Commun. 18, 303–307 (1965).

    Article  Google Scholar 

  90. —: Pyruvate: Ferredoxin oxido-reductase from Clostridium acidi-urici. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 189–198 (1965).

    Google Scholar 

  91. San Pietro, A.: Ed. Non-Heme Iron Proteins: Role in Energy Conversion, Antioch Press, Yellow Springs, Ohio (1965).

    Google Scholar 

  92. — and C. C. Black: Enzymology of energy conversion in photosynthesis. Ann. Rev. Plant Physiol. 16, 155–174 (1965).

    Article  CAS  Google Scholar 

  93. — and H. M. Lang: Accumulation of reduced pyridine nucleotides by illuminated grana. Science 124, 118–119 (1956).

    Article  CAS  Google Scholar 

  94. —: Photosynthetic pyridine nucleotide reductase. I. Partial purification and properties of the enzyme from spinach. J. Biol. Chem. 231, 211–229 (1958).

    CAS  Google Scholar 

  95. Shapiro, D. M.: The purification and properties of photosynthetic pyridine nucleotide reductase from Euglena gracilis. Doctoral Thesis, Johns Hopkins University, Baltimore, Md. Quoted by San Pietro and Black (1965) (1961).

    Google Scholar 

  96. Shashoua, V. E.: Formamidine sulfinic acid as a biochemical reducing agent. Biochemistry 3, 1719–1720 (1964).

    Article  CAS  Google Scholar 

  97. Shetna, Y. I., P. W. Wilson, R. E. Hansen, and H. Beinert: Identification by isotopic substitution of the EPR signal at g=1.94 in a non-heme iron protein from Azotobacter. Proc. Natl. Acad. Sci. (U. S.) 52, 1263–1271 (1964).

    Article  Google Scholar 

  98. Shin, M. and D. I. Arnon: Enzymic mechanisms of pyridine nucleotide reduction in chloroplasts. J. Biol. Chem. 240, 1405–1411 (1965).

    CAS  Google Scholar 

  99. —, K. Tagawa, and D. I. Arnon: Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts. Biochem. Z. 338, 84–96 (1963).

    CAS  Google Scholar 

  100. Sieker, L. C. and L. H. Jensen: An X-ray investigation of the structure of a bacterial ferredoxin. Biochem. Biophys. Res. Commun. 20, 33–35 (1965).

    Article  CAS  Google Scholar 

  101. Smillie, R. M.: Isolation of two proteins with chloroplast ferredoxin activity from a blue-green alga. Biochem. Biophys. Res. Commun. 20, 621–629 (1965).

    Article  CAS  Google Scholar 

  102. Sobel, B. E. and W. Lovenberg: Characteristics of Clostridium pasteurianum ferredoxin in oxidation-reduction reactions. Biochemistry 5, 6–13 (1966).

    Article  CAS  Google Scholar 

  103. Stadtman, E. R. and H. A. Barker: Fatty acid synthesis by enzyme preparations of Clostridium kluyveri. VI. Reactions of acyl phosphates. J. Biol. Chem. 184, 769–793 (1950).

    CAS  Google Scholar 

  104. Stern, J. R.: Role of cofactors in pyruvate oxidation and synthesis by extracts of Clostridium kluyveri. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 199–210 (1965).

    Google Scholar 

  105. Tagawa, K. and D. I. Arnon: Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature 195, 537–543 (1962).

    Article  CAS  Google Scholar 

  106. Tanaka, M., A. M. Benson, H. F. Mower, and K. T. Yasunobu: A proposed structure of C. pasteurianum ferredoxin. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 221–224 (1965).

    Google Scholar 

  107. —, T. Nakashima, A. Benson, H. Mower, and K. T. Yasunobu: The amino acid sequence of Clostridium pasteurianum ferredoxin. Biochemistry 5, 1666–1681 (1966).

    Article  CAS  Google Scholar 

  108. —, T. Nakashima, A. M. Benson, H. F. Mower, and K. T. Yasunobu: The amino acid sequence of Clostridium pasteurianum ferredoxin. Biochem. Biophys. Res. Commun. 16, 422–427 (1964).

    Article  CAS  Google Scholar 

  109. Tomlinson, N.: Carbon dioxide and acetate utilization by Clostridium kluyveri. II. Synthesis of amino acids. J. Biol. Chem. 209, 597–603 (1954).

    CAS  Google Scholar 

  110. Tsugita, A., K. Tagawa, and D. I. Arnon: Protein chemistry of spinach ferredoxin. Abstr. Pacific Slope Biochem. Conf., Honolulu, 1963. (Sympos. on Ferredoxins, sponsored by Natl. Sci. Found.) (1963).

    Google Scholar 

  111. Ulmer, D. D. and B. L. Vallee: Optically active chromophores. III. Heme and nonheme iron proteins. Biochemistry 2, 1335–1340 (1963).

    Article  CAS  Google Scholar 

  112. —: Extrinsic cotton effects and the mechanism of enzyme action. Advan. Enzymol. 27, 37–104 (1965).

    CAS  Google Scholar 

  113. Valentine, R. C.: Bacterial ferredoxin. Bacteriol. Rev. 28, 497–517 (1964).

    CAS  Google Scholar 

  114. —, W. J. Brill, and R. S. Wolfe: Role of ferredoxin in pyridine nucleotide reduction. Proc. Natl. Acad. Sci. (U. S.) 48, 1856–1860 (1962).

    Article  CAS  Google Scholar 

  115. —, R. L. Jackson, and R. S. Wolfe: Role of ferredoxin in hydrogen metabolism of Micrococcus lactilyticus. Biochem. Biophys. Res. Commun. 7, 453–456 (1962).

    Article  CAS  Google Scholar 

  116. —, L. E. Mortenson, H. F. Mower, R. L. Jackson, and R. S. Wolfe: Ferredoxin requirement for reduction of hydroxylamine by Clostridium pasteurianum. J. Biol. Chem. 238, PC856 (1963).

    Google Scholar 

  117. — and R. S. Wolfe: Role of ferredoxin in the metabolism of molecular hydrogen. J. Bacteriol. 85, 1114–1120 (1963).

    CAS  Google Scholar 

  118. Vallee, B. L. and D. D. Ulmer: Optical rotatory dispersion of iron proteins. In Non-Heme Iron Proteins: Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 43–68 (1965).

    Google Scholar 

  119. Weaver, P., K. Tinker, and R. C. Valentine: Ferredoxin linked DPN reduction by the photosynthetic bacteria Chromatium and Chlorobium. Biochem. Biophys. Res. Commun. 21, 195–201 (1965).

    Article  CAS  Google Scholar 

  120. Wolfe, R. S. and D. J. O’Kane: Cofactors of the phosphoroclastic reaction of Clostridium butyricum. J. Biol. Chem. 205, 755–765 (1953).

    CAS  Google Scholar 

  121. Whatley, F. R., K. Tagawa, and D. I. Arnon: Separation of the light and dark reactions in electron transfer during photosynthesis. Proc. Natl. Acad. Sci. (U. S.) 49, 266–270 (1963).

    Article  CAS  Google Scholar 

  122. Yamanaka, T. and M. D. Kamen: Purification of an NADP-reductase and of ferredoxin derived from the facultative photoheterotroph, Rhodopseudomonas palustris. Biochem. Biophys. Res. Commun. 18, 611–616 (1965).

    Article  CAS  Google Scholar 

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Buchanan, B.B. (1966). The chemistry and function of ferredoxin. In: Structure And Bonding. Structure and Bonding, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0119550

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