The Chloroplast b Cytochromes: Crosslinks, Topography, and Functions

  • W. A. Cramer
  • P. N. Furbacher
  • A. Szczepaniak
  • G.-S. Tae

Abstract

Heme cross-linking of membrane cytochromes as a structural principle: cytochrome b-559, b 6 , and cytochrome oxidase. After the Mr 9,000 protein of cyt b–559 was purified and its NH2-terminus sequenced (1), its psbE gene and the downstream psbF gene located and sequenced on the spinach chloroplast genome (2), an intermolecular heme cross-linked dimeric structure of cytochrome b–559 was proven by the findings that (a) each polypeptide contains only one histidine (2), (b) the psbE and psbF gene products are present in the purified protein in a 1:1 stoichiometry (3), and (c) the heme coordination is bis-histidine (Fig. la; ref. 4). Thus, a dimer would be required to provide two His residues for heme coordination. There are several reasons, including the 1:1 stoichiometry, for believing that the heme-binding unit is an α-β heterodimer (5), but this has not been rigorously proven.

Keywords

Cyclic Electron Transport Fatty Acid Desaturation Lumen Side Stromal Side Quinone Binding Site 
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.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • W. A. Cramer
    • 1
  • P. N. Furbacher
    • 1
  • A. Szczepaniak
    • 1
  • G.-S. Tae
    • 1
  1. 1.Dept. of Biological SciencesPurdue UniversityWest LafayetteUSA

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