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Biochemical aspects of iron-sulfur linkage in non-heme iron protein, with special reference to “Adrenodoxin”

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Structure and Bonding

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Abbreviations

AS:

ammonium sulfate

DEAE-cellulose:

diethyl-aminoethyl-cellulose

NADPH:

reduced nicotinamide adenine dinucleotide phosphate

References

  1. Atherton, N. M., K. Garbett, R. D. Gillard, R. Mason, S. J. Mayhew, J. L. Peel, and J. E. Stangroom: Spectroscopic investigation of rubredoxin and ferredoxin. Nature 212, 590 (1966).

    Article  CAS  Google Scholar 

  2. Bachmayer, H., and K. T. Yasunobu: The amino acid sequence of micrococcus aerogenes rubredoxin. Biochem. Biophys. Res. Commun. 26, 435 (1967).

    Article  CAS  Google Scholar 

  3. —, L. H. Piette, and K. T. Yasunobu: The binding sites of iron in rubredoxin. Proc. Natl. Acad. Sci. U.S. 57, 122 (1967).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  5. Bayer, E., D. Josef, P. Krauss, H. Hagenmaier, A. Röder u. A. Trebst: Abbau und Resynthese des Aktiventrums vom Pflanzenferredoxin. Biochim. Biophys. Acta 143, 435 (1967).

    Article  CAS  Google Scholar 

  6. —, and N. Parr: Eliminierung von Schwefelwasserstoff aus Ferredoxin und Cysteinmethylester. Angew. Chem. 78, 824 (1966).

    Article  CAS  Google Scholar 

  7. —, and B. Kazmaier: Aufbau des Ferredoxins, des Wirkstoffes, der Assimilations-Vorgänge. Arch. Pharm. 298, 196 (1965).

    Article  CAS  Google Scholar 

  8. Bearden, A. J., T. H. Moss, R. G. Bartsh, and M. A. Cusanovich: Mössbauer spectroscopy studies of chromatium non-heme iron protein. In: Non-heme iron proteins. p. 87; A. San Pietro, ed. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

  9. Beinert, H.: EPR spectroscopy in the detection, study and identification of protein-bound non-heme iron. In: Non-heme iron proteins, p. 23; A. San Pietro, ed. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

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

    Article  CAS  Google Scholar 

  11. Brintzinger, H., G. Palmer, and R. H. Sands: On the ligand field of iron in ferredoxin from spinach chloroplasts and related non-heme iron protein. Proc. Natl. Acad. Sci. U.S., 55, 397 (1966).

    Article  CAS  Google Scholar 

  12. Buchanan, B.B.: The chemistry and function of ferredoxin. Struct. Bonding 1, 109 (1966).

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  14. Cushman, D. W., R. L. Tsai, and I. C. Gunsalus: The ferroprotein component of a methylene hydroxylase. Biochem. Biophys. Res. Commun. 26, 577 (1967).

    Article  CAS  Google Scholar 

  15. Der Vartanian, D. V., W. H. Orme-Johnson, R. E. Hansen, and H. Beinert: Identification of sulfur as component of the EPR signal at g=1.94 by isotopic sulfur. Biochem. Biophys. Res. Commun. 26, 569 (1967).

    Article  Google Scholar 

  16. Dus, K., H. De Klerk, K. Sletten, and R. G. Bartsh: Chemical characterization of high potential iron proteins from chromatium and rhodopseudomonas gelatinosa. Biochim. Biophys. Acta 140, 291 (1967).

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  18. Fry, K. T., and A. San Pietro: Studies on photosynthetic pyridine nucleotide reductase. Biochem. Biophys. Res. Commun. 9, 218 (1962).

    Article  CAS  Google Scholar 

  19. Gewitz, H. S., u. W. Völker: Über die Atmungsfermente der Chlorella. Z. Physiol. Chem. 330, 124 (1962).

    CAS  Google Scholar 

  20. Gibson, J. F., D. O. Hall, J. H. M. Thornley, and F. R. Whatley: The iron complex in spinach ferredoxin. Proc. Natl. Acad. Sci. U.S. 56, 987 (1966).

    Article  CAS  Google Scholar 

  21. Hong, J. S., and J. C. Rabinowitz: Preparation and properties of clostridial apoferredoxins. Biochem. Biophys. Res. Commun. 29, 246 (1967).

    Article  CAS  Google Scholar 

  22. Kawamura, S., Y. Otsuji, T. Nakabayashi, T. Kitao, and J. Tsurugi: Aralkyl hydrodisulfides. IV. The reaction of benzyl hydrosdisulfide with several nucleophiles. J. Org. Chem. 30, 2711 (1965).

    Article  CAS  Google Scholar 

  23. Keresztes-Nagy, S., and E. Margoliash: Preparation and characterization of alfalfa ferredoxin. J. Biol. Chem. 241, 5955 (1966).

    CAS  Google Scholar 

  24. Kimura, T.: In: A symposium on biogenesis and action of steroid hormones, Yonago, Japan, August, 1967, in press.

    Google Scholar 

  25. Kimura, T. In: A symposium on function of adrenal cortex, Gainesville, Florida, U.S.A., November, 1966, in press.

    Google Scholar 

  26. —: Redox components of adrenal steroid hydroxylase. In: biological and chemical aspects of oxygenases, p. 179. K. Bloch and O. Hayaishi, ed. Tokyo: Maruzen 1966.

    Google Scholar 

  27. —: Studies on steroid hydroxylases. J. Japan. Biochem. 38, 209 (1966).

    CAS  Google Scholar 

  28. —, and H. Ohno: Preparation of testis non-heme iron protein and substitution for adrenodoxin by various non-heme iron proteins in steroid 11 β-hydroxylation. J. Biochem. 63, 716 (1968).

    CAS  Google Scholar 

  29. —, and K. Suzuki: Components of the electron transport system in adrenal steroid hydroxylase. J. Biol. Chem. 242, 485 (1967).

    CAS  Google Scholar 

  30. —: Enzymatic reduction of non-heme iron protein (adrenodoxin) by reduced nicotinamide adenine dinucleotide phosphate. Biochem. Biophys. Res. Commun. 20, 373 (1965).

    Article  CAS  Google Scholar 

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

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  34. —: Non-heme iron electron-transfer proteins. Ann. Rev. Biochem. 36, 113 (1967).

    Article  CAS  Google Scholar 

  35. —: The reactivity of clostridial ferredoxin with iron chelating agents and 5,5′-dithio-bis-2-nitrobenzoic acid. Biochemistry 6, 3880 (1967).

    Article  CAS  Google Scholar 

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

    CAS  Google Scholar 

  37. —: The role of iron in beef-heart succinic dehydrogenase, Biochim Biophys. Acta 30, 500 (1958).

    Article  CAS  Google Scholar 

  38. Matsubara, H., R. M. Sasaki, and R. K. Chain: The amino acid sequence of spinach ferredoxin. Proc. Natl. Acad. Sci. U. S. 57, 439 (1967).

    Article  Google Scholar 

  39. Miller, R. W., and V. Massey: Dihydroorotic dehydrogenase. I. Some properties of the enzyme. J. Biol. Chem. 240, 1453 (1965).

    CAS  Google Scholar 

  40. Nagai, J., and K. Bloch: Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 241, 1925 (1966).

    CAS  Google Scholar 

  41. —: Synthesis of oleic acid by euglena gracilis. J. Biol. Chem. 240, PC3702 (1965).

    Google Scholar 

  42. Nakabayashi, T., J. Tsurugi, S. Kawamura, T. Kitao, M. Ui, and M. Nose: Aralkyl hydrodisulfides. VII. The reaction with trisubstituted phosphines. J. Org. Chem. 31, 4174 (1966).

    Article  CAS  Google Scholar 

  43. Ohno, H., K. Suzuki, and T. Kimura: A non-heme iron protein from pig testis and its substitution for adrenal non-heme iron protein (adrenodoxin) in steroid 11β-hydroxylation. Biochem. Biophys. Res. Commun. 26, 651 (1967).

    Article  CAS  Google Scholar 

  44. Omura, T., R. Sato, D. Y. Cooper, O. Rosenthal, and R. W. Estabrook: Function of cytochrome P-450 in microsomes. Federation Proc. 24, 1181 (1965).

    CAS  Google Scholar 

  45. —, E. Sanders, D. Y. Cooper, and R. W. Estabrook: Isolation of adrenal cortex non-heme iron protein. Methods in Enzymol., vol. 10 p. 362. New York: Academic Press 1967.

    Google Scholar 

  46. —, and R. W. Estabrook: Isolation from adrenal cortex of a non-heme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotidecytochrome P-450 reductase. Arch. Biochem. Biophys. 117, 660 (1966).

    Article  CAS  Google Scholar 

  47. —, D. Y. Cooper, O. Rosenthal, and R. W. Estabrook: Isolation of a non-heme iron protein of adrenal cortex functional as a TPNH-flavoprotein-cytochrome P-450 reductase for hydroxylation reaction. In: Non-heme iron proteins, p. 401; A. San Pietro, ed. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

  48. Palmer, G.: The effect of the Fe57 hyperfine interaction on the EPR spectrum of spinach ferredoxin. Biochem. Biophys. Res. Commun. 27, 315 (1967).

    Article  CAS  Google Scholar 

  49. —, H. Brinzinger, and R. W. Estabrook: Spectroscopic studies on spinach ferredoxin and adrenodoxin. Biochemistry 6, 1658 (1967).

    Article  CAS  Google Scholar 

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

    CAS  Google Scholar 

  51. —, and L. E. Mortenson: Electron paramagnetic resonance study on the ferredoxin from clostridium pasteurianum. Biochem. Biophys. Res. Commun. 23, 357 (1966).

    Article  CAS  Google Scholar 

  52. Peterson, J. A., D. Basu, and M. J. Coon: Enzymatic ω-oxidation. 1. Electron carrier in fatty acid and hydrocarbon hydroxylation. J. Biol. Chem. 241, 5162 (1966).

    CAS  Google Scholar 

  53. —, M. Kusunose, E. Kusunose, and M. J. Coon: Enzymatic ω-oxidation. II. Function of rubredoxin as the electron carrier in ω-hydroxylation. J. Biol. Chem. 242, 4334 (1967).

    CAS  Google Scholar 

  54. Phillips, W. D., E. Knight, Jr., and D. C. Blomstrom: Fe57 Mössbauer spectroscopy and some biological applications. In: Non-heme iron proteins, p. 69; A San Pietro, ed. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

  55. Rieske, J. S., D. H. Maclennan, and R. Coleman: Isolation and properties of an iron-protein from the (reduced-coenzyme Q)-cytochrome c reductase complex of the respiratory chain. Biochem. Biophys. Res. Commun. 15, 338 (1964).

    Article  Google Scholar 

  56. San Pietro, A.: Non-heme iron proteins. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

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

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  59. Suzuki, K.: Sulfhydryl groups of iron environment in non-heme iron protein (adrenodoxin) as an oxidation-reduction component of steroid 11 β-hydroxylase from adrenal mitochondria. Biochemistry 6, 1335 (1967).

    Article  CAS  Google Scholar 

  60. —, and T. Kimura: An iron protein as a component of steroid 11 β-hydroxylase complex. Biochem. Biophys. Res. Commun., 19, 340 (1965).

    Article  CAS  Google Scholar 

  61. —: Detection of labile sulfide in serum albumin. Biochem. Biophys. Res. Commun. 28, 514 (1967).

    Article  CAS  Google Scholar 

  62. Suzuki, K. T. Kimura unpublished data.

    Google Scholar 

  63. Tagawa, K., and D. I. Arnon: Ferredoxin as electron carriers in photosynthesis and its biological production and consumption of hydrogen gas. Nature 195, 537 (1962).

    Article  CAS  Google Scholar 

  64. Tanaka, M., A. M. Benson, H. F. Mower, and K. T. Yasunobu: A proposed structure of C. pasteurianum ferredoxin. In: Non-heme iron proteins, p. 221; A. San Pietro, ed. Yellow Springer, Ohio: Antioch Press 1965.

    Google Scholar 

  65. —, T. Nakashima, A. Benson, H. F. Mower, and K. T. Yasunobu The amino acid sequence of clostridium pasteurianum ferredoxin. Biochem. Biophys. Res. Commun. 16, 422 (1964).

    Article  CAS  Google Scholar 

  66. —: The amino acid sequence of clostridium pasteurianum ferredoxin. Biochemistry, 5, 1666 (1966).

    Article  CAS  Google Scholar 

  67. Vallee, B. L., and D. D. Ulmer: Optical rotatory dispersion of iron proteins. In: Non-heme iron proteins, p. 43; A. San Pietro, ed. Yellow Springs, Ohio: Antioch Press 1965.

    Google Scholar 

  68. Watari, H., and T. Kimura: Study of the adrenal non-heme iron protein (adrenodoxin) by electron spin resonance. Biochem. Biophys. Res. Commun. 24, 106 (1966).

    Article  CAS  Google Scholar 

  69. Watari, H., T. Kimura, and A. Tasaki, Biochim. Biophys. Acta, to be published.

    Google Scholar 

  70. Yamano, T.: a personal communication.

    Google Scholar 

  71. Seventh international congress of biochemistry, Tokyo, Japan, 1967.

    Google Scholar 

  72. unpublished data from this laboratory.

    Google Scholar 

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Kimura, T. (1968). Biochemical aspects of iron-sulfur linkage in non-heme iron protein, with special reference to “Adrenodoxin”. In: Structure and Bonding. Structure and Bonding, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0118845

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  • DOI: https://doi.org/10.1007/BFb0118845

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