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Energy Coupling to Pyridine Nucleotide Transhydrogenase in Chromatophores from Phototrophic Bacteria

  • B. F. Nore
  • T. M. Lever
  • N. P. J. Cotton
  • M. R. Jones
  • J. B. Jackson
Part of the NATO ASI Series book series (NSSA, volume 168)

Abstract

The membrane-bound pyridine nucleotide transhydrogenase of Rhodobacter capsulatus catalysing the reaction, like that from mitochondria and from E. coli, is a consumer of Ap in the direction from left to right. It offers several important advantages in the study of energy coupling (1).

Keywords

Energy Coupling Similar Experimental Condition Pyridine Nucleotide PHOTOTROPHIC Bacterium Photosynthesis Research 
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.

References

  1. (1).
    Fisher, R.R. and Earle, S.R. (1982) in The Pyridine Nucleotide Coenzymes, pp.279–324, Academic Press.Google Scholar
  2. (2).
    Cotton, N.P.J. and Jackson, J.B. (1988) FEBS Lett. 229, 303–307.CrossRefGoogle Scholar
  3. (3).
    Cotton, N.P.J., Myatt, J.F. and Jackson, J.B. (1987) FEBS Lett. 219, 88–92.CrossRefGoogle Scholar
  4. (4).
    Rydsröm, J., Teixeria da Cruz, A. and Ernster, L. (1970) Eur. J. Biochem. 17, 56–62.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • B. F. Nore
    • 1
  • T. M. Lever
    • 2
  • N. P. J. Cotton
    • 2
  • M. R. Jones
    • 2
  • J. B. Jackson
    • 2
  1. 1.Department of BiochemistryUniversity of StockholmStockholmSweden
  2. 2.University of BirminghamBirminghamUK

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