Advertisement

Transhydrogenase

  • P. Böger
Part of the Encyclopedia of Plant Physiology book series (PLANT, volume 6)

Abstract

This chapter deals with nicotinamide nucleotide transhydrogenases, E.C.1.6.1.1 (pyridine nucleotide oxidoreductase) which catalyze hydrogen transfer between two pyridine nucleotides:
$$ {\text{NADPH + NA}}{{\text{D}}^{\text{ + }}} \rightleftharpoons {\text{NAD}}{{\text{P}}^{\text{ + }}}{\text{ + NADH}} $$
(1)
According to the source of the enzyme the reaction may or may not be reversible, and since definite specificity is lacking, the hydrogen acceptor may be generally substituted for by various nucleotide analogs such as thionicotinamide NAD(P)+ [=TN-NAD(P)+] or 3-acetylpyridine-adenine dinucleotide (phosphate). TNNAD(P)H has an absorption peak at 400 nm (ε=11.3 mM−1·cm−1), which often allows convenient determination of the reduced mother compounds in addition to the analog (Cohen and Kaplan, 1970b; Böger, 1972a). A transhydrogenase reaction as defined here does not imply a third substrate mediating hydrogen transfer as, for example, malate in malate/lactate “transhydrogenase” (Allen and Paul, 1972) or glutamate in glutamic dehydrogenases which are unspecific for pyridine nucleotides.

Keywords

Hydrogen Transfer Photosynthetic Bacterium Pyridine Nucleotide Spinach Chloroplast Rhodopseudomonas Palustris 
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. Allen, S.H.G., Patil, J.R.: J. Biol. Chem. 247, 909–916 (1972)PubMedGoogle Scholar
  2. Ammeraal, R.N., Krakow, G., Vennesland, B.: J. Biol. Chem. 240, 1824–1828 (1965)PubMedGoogle Scholar
  3. Anderson, W.M., Fisher, R.R.: Arch. Biochem. Biophys. 187, 180–190 (1978)PubMedCrossRefGoogle Scholar
  4. Berger, T.J., Orlando, J.A.: Arch. Biochem. Biophys. 159, 25–31 (1973)PubMedCrossRefGoogle Scholar
  5. Blazyk, J.F., Fisher, R.R.: FEBS Lett. 50, 227–232 (1975)PubMedCrossRefGoogle Scholar
  6. Böger, P.: Planta (Berl.) 99, 319–338 (1971a)CrossRefGoogle Scholar
  7. Böger, P.: Z. Naturforsch. 26b, 807–815 (1971b)Google Scholar
  8. Böger, P.: Z. Naturforsch. 27b, 826–833 (1972a)Google Scholar
  9. Böger, P.: In: Proc. 2nd Int. Congr. Photosynthesis. Forti, G. et al. (eds.), Vol. I, pp. 449–458. The Hague: Junk N. V. Publ. 1972bGoogle Scholar
  10. Böger, P., Lien, S.S., San Pietro, A.: Z. Naturforsch. 28c, 505–510 (1973)Google Scholar
  11. Böhme, H.: In: Membrane bioenergetics. Packer, L. et al. (eds.), pp. 329–337. Amsterdam: Elsevier-North Holland 1977Google Scholar
  12. Böhme, H.: Eur. J. Biochem. 83, 137–141 (1978)PubMedCrossRefGoogle Scholar
  13. Bookjans, G., Böger, P.: Arch. Biochem. Biophys. 190, 459–465 (1978)PubMedCrossRefGoogle Scholar
  14. Bookjans, G., Böger, P.: Arch. Biochem. Biophys. (1979), in pressGoogle Scholar
  15. Bookjans, G., San Pietro, A., Böger, P.: Biochem. Biophys. Res. Commun. 80, 759–765 (1978)PubMedCrossRefGoogle Scholar
  16. Bragg, P.D., Hou, C.: FEBS Lett. 28, 309–312 (1972)PubMedCrossRefGoogle Scholar
  17. Buchanan, B.B., Bachofen, R.: Biochim. Biophys. Acta 162, 607–610 (1968)PubMedCrossRefGoogle Scholar
  18. Chopowick, R., Israelstamm, G.F.: Planta (Berl.) 101,171–173 (1973)CrossRefGoogle Scholar
  19. Chung, A.E.: J. Bacteriol. 102, 438–447 (1970)PubMedGoogle Scholar
  20. Cohen, P.T., Kaplan, N.O.: J. Biol. Chem. 245, 2825–2836 (1970a)Google Scholar
  21. Cohen, P.T., Kaplan, N.O.: J. Biol. Chem. 245, 4666–4682 (1970b)Google Scholar
  22. Cox, G.B., Gibson, R., McCann, L.M., Butlin, J.D., Crane, F.L.: Biochem. J. 132, 689–695 (1973)PubMedGoogle Scholar
  23. Davis, D.J., San Pietro, A.: Biochem. Biophys. Res. Commun. 74, 33–40 (l977a)CrossRefGoogle Scholar
  24. Davis, D.J., San Pietro, A.: Arch. Biochem. Biophys. 182, 266–272 (1977b)CrossRefGoogle Scholar
  25. Djavadi-Ohaniance, L., Hatefi, Y.: J. Biol. Chem. 250, 9397–9403 (1975)PubMedGoogle Scholar
  26. Dontsov, A.E., Grinius, L.L., Jasaitis, A.A., Severina, I.I., Skulachev, C.P.: J. Bioenerg. 3, 277–303 (1972)PubMedCrossRefGoogle Scholar
  27. Earle, S.R., Anderson, W.M., Fisher, R.R.: FEBS Lett. 91, 21–24 (1978)PubMedCrossRefGoogle Scholar
  28. Ernster, L.: Annu. Rev. Biochem. 33, 729–788 (1964)PubMedCrossRefGoogle Scholar
  29. Ernster, L., Juntti, K., Asami, K.: J. Bioenerg. 4,149–159 (1973)PubMedCrossRefGoogle Scholar
  30. Fisher, R.R., Guillory, R.J.: J. Biol. Chem. 244, 1078–1079 (1969)PubMedGoogle Scholar
  31. Fisher, R.R., Guillory, R.J.: J. Biol. Chem. 246, 4679–4686 (1971a)Google Scholar
  32. Fisher, R.R., Guillory, R.J.: J. Biol. Chem. 246, 4687–4693 (1971b)Google Scholar
  33. Fisher, R.R., Kaplan, N.O.: Biochemistry 12,1182–1188 (1973)PubMedCrossRefGoogle Scholar
  34. Fisher, R.R., Rampey, S.A., Sadighi, A., Fisher, K.: J. Biol. Chem. 250, 819–825 (1975)PubMedGoogle Scholar
  35. Forti, G.: Encyclopedia of plant physiology. Photosynthesis I, Trebst, A., Avron, M. (eds.), Vol. 5, pp. 222–226. Berlin, Heidelberg, New York: Springer 1977Google Scholar
  36. Foust, G.P., Mayhew, S.G., Massey, V.: J. Biol. Chem. 244, 964–970 (1969)PubMedGoogle Scholar
  37. Fredericks, W.W., Gehl, J.M.: J. Biol. Chem. 246, 1201–1205 (1971)Google Scholar
  38. Green, W.G.E., Israelstamm, G.F.: Physiol. Plant. 23, 217–231 (1970)CrossRefGoogle Scholar
  39. Griffiths, D.E., Robertson, A.M.: Biochim. Biophys. Acta 118, 453–464 (1966)PubMedGoogle Scholar
  40. Guillory, R.J., Fisher, R.R.: FEBS Lett. 3, 27–30 (1969)PubMedCrossRefGoogle Scholar
  41. Haslett, B.G., Cammack, R.: New Phytol. 76,219–226 (1976)CrossRefGoogle Scholar
  42. Hatefi, Y., Galante, Y.M.: Proc. Natl. Acad. Sci. USA 74, 846–850 (1977)PubMedCrossRefGoogle Scholar
  43. Höjeberg, B., Rydström, J.: Biochem. Biophys. Res. Commun. 78, 1183–1190 (1977)PubMedCrossRefGoogle Scholar
  44. Hoek, J.B., Rydström, J., Höjeberg, B.: Biochim. Biophys. Acta 333, 237–245 (1974)PubMedCrossRefGoogle Scholar
  45. Jacobs, E., Heriot, K., Fisher, R.R.: Arch. Microbiol. 115, 151–156 (1977)PubMedCrossRefGoogle Scholar
  46. Jungermann, K., Rupprecht, E., Ohrloff, C., Thauer, R., Decker, K.: J. Biol. Chem. 246, 960–963 (1971)PubMedGoogle Scholar
  47. Kaplan, N.O.: Methods Enzymol. 10, 317–322 (1967)CrossRefGoogle Scholar
  48. Kaufman, B., Kaplan, N.O.: J. Biol. Chem. 236, 2133–2139 (1961)PubMedGoogle Scholar
  49. Kawasaki, T., Satoh, K., Kaplan, N.O.: Biochem. Biophys. Res. Commun. 17, 648–654 (1964)CrossRefGoogle Scholar
  50. Keister, D.L., Hemmes, R.B.: J. Biol. Chem. 241, 2820–2825 (1966)PubMedGoogle Scholar
  51. Keister, D.L., San Pietro, A., Stolzenbach, F.E.: J. Biol. Chem. 235, 2989–2996 (1960a)Google Scholar
  52. Keister, D.L., San Pietro, A., Stolzenbach, F.E.: Arch. Biochem. Biophys. 98,235–244 (1960b)CrossRefGoogle Scholar
  53. Keister, D.L., Yike, N.J.: Biochemistry 6, 3847–3857 (1967)PubMedCrossRefGoogle Scholar
  54. Knobloch, K.: Z. Naturforsch. 30e, 771–776 (1975)Google Scholar
  55. Kohler, P., Saz, H.J.: J. Biol. Chem. 251, 2217–2225 (1976)PubMedGoogle Scholar
  56. Konings, A.W.T., Guillory, R.J.: J. Biol. Chem. 248, 1045–1050 (1973)PubMedGoogle Scholar
  57. Kramar, R., Salvenmoser, F.: Hoppe Seyler’s Z. Physiol. Chem. 346, 310–313 (1966)Google Scholar
  58. Krause, G.H., Heber, U.: In: The intact chloroplast. Barber, J. (ed.), pp. 171–214. Amsterdam, New York, Oxford: Elsevier 1976Google Scholar
  59. Krawetz, S.A., Israelstamm, G.F.: Plant Sci. Lett. 12, 323–326 (1978)CrossRefGoogle Scholar
  60. Kusai, A., Yamanaka, T.: Biochim. Biophys. Acta 292, 621–633 (1973)PubMedCrossRefGoogle Scholar
  61. Lee, C.P., Ernster, L.: Biochim. Biophys. Acta 81, 187–190 (1964)Google Scholar
  62. Lee, C.P., Ernster, L.: In: Regulation of metabolic processes in mitochondria. Tager, J.M. et al. (eds.), pp. 218–234. Amsterdam: Elsevier 1966Google Scholar
  63. Lee, C.P., Azzone, G.F., Ernster, L.: Nature (London) 201,152–155 (1964)CrossRefGoogle Scholar
  64. Lee, C.P., Simard-Duquesne, N., Ernster, L.: Biochim. Biophys. Acta 105, 397–409 (1965)PubMedGoogle Scholar
  65. Lendzian, K., Bassham, J.A..: Biochim. Biophys. Acta 430, 478–489 (1976)PubMedCrossRefGoogle Scholar
  66. Louie, D.D., Kaplan, N.O.: J. Biol. Chem. 245, 5691–5698 (1970)PubMedGoogle Scholar
  67. McFadden, B.J., Fisher, R.R.: Arch. Biochem. Biophys. 190, 820–828 (1978)PubMedCrossRefGoogle Scholar
  68. Middleditch, L.E., Chung, A.E.: Arch. Biochem. Biophys. 146, 449–453 (1971)PubMedCrossRefGoogle Scholar
  69. Nakamura, S., Kimura, T.: J. Biol. Chem. 246, 6235–6241 (1971a)Google Scholar
  70. Nakamura, S., Kimura, T.: FEBS Lett. 15, 352–354 (1971b)CrossRefGoogle Scholar
  71. Nakamura, S., Kimura, T.: J. Biol. Chem. 247, 6462–6468 (1972)PubMedGoogle Scholar
  72. Nakamura, S., Kazim, A.L., Wang, H.P., Chu, J.W., Kimura, T.: FEBS Lett. 28, 209–212 (1972)PubMedCrossRefGoogle Scholar
  73. Nelson, N., Neumann, J.: J. Biol. Chem. 244, 1926–1931 (1969); 244, 1932–1936PubMedGoogle Scholar
  74. Orlando, J.A., Sabo, D., Curnyn, C.: Plant. Physiol. 41, 937–945 (1966)PubMedCrossRefGoogle Scholar
  75. Ostroumov, S.A., Samuilov, V.P., Skulachev, V.P.: FEBS Lett. 31, 27–29 (1973)PubMedCrossRefGoogle Scholar
  76. Palmer, G., Massey, M.: In: Biological oxidations. Singer, Th.P. (ed.), pp.263–300. New York, London, Sydney: Interscience Publ. 1968Google Scholar
  77. Petitdemange, H., Bengone, J.M., Bergere, J.L., Gay, R.: Biochimie 55, 1307–1310 (1973)PubMedCrossRefGoogle Scholar
  78. Ragan, C.I., Widger, W.R.: Biochem. Biophys. Res. Commun. 62, 744–749 (1975)PubMedCrossRefGoogle Scholar
  79. Rydström, J.: Eur. J. Biochem. 31, 496–504 (1972)PubMedCrossRefGoogle Scholar
  80. Rydström, J.: Biochim. Biophys. Acta 463, 155–184 (1977)PubMedGoogle Scholar
  81. Rydström, J., Teixeira da Cruz, A., Ernster, L.: Eur. J. Biochem. 17, 56–62 (1970)PubMedCrossRefGoogle Scholar
  82. Rydström, J., Panov, A.V., Paradies, G., Ernster, L.: Biochem. Biophys. Res. Commun. 45, 1389–1397 (1971a)CrossRefGoogle Scholar
  83. Rydström, J., Teixeira da Cruz, A., Ernster, L.: Eur. J. Biochem. 23, 212–219 (1971b)CrossRefGoogle Scholar
  84. Rydström, J., Hoek, J., Höjeberg, B.: Biochem. Biophys. Res. Commun. 52, 421–429 (1973)PubMedCrossRefGoogle Scholar
  85. Rydström, J., Hoek, J.B., Ernster, L.: In: The enzymes. 3rd ed. Boyer, P.D. (ed.), Vol. XIII, pp. 51–88. New York, London: Academic Press 1976Google Scholar
  86. Sabet, S.F.: J. Bacteriol. 129, 1397–1406 (1977)PubMedGoogle Scholar
  87. Salvenmoser, F., Kramar, R.: Enzymologia 40, 322–327 (1971)PubMedGoogle Scholar
  88. Schneeman, R., Krogmann, D.W.: J. Biol. Chem. 250,4965–4971 (1975)PubMedGoogle Scholar
  89. Shin, M., Arnon, D.I.: J. Biol. Chem. 240, 1405–1411 (1965)PubMedGoogle Scholar
  90. Shin, M., San Pietro, A.: Biochem. Biophys. Res. Commun. 33, 38–42 (1968)PubMedCrossRefGoogle Scholar
  91. Shin, M., Tagawa, K., Arnon, D.I.: Biochem. Z. 338, 84–96 (1963)PubMedGoogle Scholar
  92. Singh, A.P., Bragg, P.D.: J. Gen. Microbiol. 82, 237–246 (1974)PubMedGoogle Scholar
  93. Spiller, H., Bookjans, G., Boger, P.: Z. Naturforsch. 31c, 565–568 (1976)Google Scholar
  94. Sweetman, A.J., Green, A.P., Hooper, M.: Biochem. Biophys. Res. Commun. 58, 337–343 (1974)PubMedCrossRefGoogle Scholar
  95. Tager, J.M., Groot, G.S.P., Roos, D., Papa, S., Quagliariello, E.: In: The energy level and metabolic control in mitochondria. Papa, S. et al. (eds.), pp. 453–466. Bari: Adriatica Editrice 1969Google Scholar
  96. Teixeira da Cruz, A., Rydström, J., Ernster, L.: Eur. J. Biochem. 23, 203–211 (1971)PubMedCrossRefGoogle Scholar
  97. Thauer, R.K., Rupprecht, E., Ohrloff, C., Jungermann, K., Decker, K.: J. Biol. Chem. 246, 954–959 (1971)PubMedGoogle Scholar
  98. Thomas, J.O., Fisher, R.R., Guillory, R.J.: Biochim. Biophys. Acta 223, 204–206 (1970)PubMedCrossRefGoogle Scholar
  99. Van den Broek, H.W.J., Veeger, C.: Eur. J. Biochem. 24, 72–82 (1971b)CrossRefGoogle Scholar
  100. Van den Broek, H.W.J., Santema, J.S., Wassink, J.H., Veeger, C.: Eur. J. Biochem. 24, 31–45 (1971a); see also 24, pp. 46–82CrossRefGoogle Scholar
  101. Van de Stadt, R.J., Niewenhuis, F.J.R.M., van Dam, K.: Biochim. Biophys. Acta 234, 173–176 (1971)PubMedCrossRefGoogle Scholar
  102. Widmer, F., Kaplan, N.O.: Biochemistry 15, 4693–4698 (1976)PubMedCrossRefGoogle Scholar
  103. Yamanaka, T., Kamen, M.D.: Biochim. Biophys. Acta 112, 436–447 (1966)CrossRefGoogle Scholar
  104. Yamanaka, T., Kamen, M.D.: Biochim. Biophys. Acta 131, 317–339 (1967)PubMedCrossRefGoogle Scholar
  105. Yoch, D.C.: J. Bacteriol. 116,384–391 (1973)PubMedGoogle Scholar
  106. Zahl, K.J., Rose, C., Hanson, R.L.: Arch. Biochem. Biophys. 190, 598–602 (1978)PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin·Heidelberg 1979

Authors and Affiliations

  • P. Böger

There are no affiliations available

Personalised recommendations