The Fatty Acid-Anchored Four Heme Cytochrome of the Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas Viridis

  • K. A. Weyer
  • F. Lottspeich
  • W. Schäfer
  • H. Michel

Abstract

The photosynthetic bacteria use a single photosystem for the absorption and conversion of solar energy. The simple structural organization of the bacterial photosynthetic reaction centers makes them useful for studying the light-driven electron transfer across the photosynthetic membrane. Photosynthetic reaction centers are complexes of pigments and integral membrane proteins. The well characterized reaction centers from the purple bacteria contain three protein subunits, which are called H (heavy), M (medium) and L (light) subunits according to their apparent molecular weights as determined by SDS-polyacrylamide gel electrophoresis1-3. In addition, the reaction centers from several purple bacteria, e.g. Rhodopseudomonas viridis contain a tightly bound cytochrome subunit, which re-reduces the photo-oxidized primary electron donor. Early work has shown that the cytochrome is of the c type and contains four (to five) heme groups. Redox potentiometry and spectroscopic studies led to the conclusion that two of these heme groups (“C558”) operate at +330 mV and the other two (“C553”) at -12mV4.5.

Keywords

Crystallization HPLC Hydrocarbon Glycine Cysteine 

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • K. A. Weyer
    • 1
  • F. Lottspeich
    • 1
  • W. Schäfer
    • 1
  • H. Michel
    • 1
  1. 1.Max-Planck-Institut für BiochemieMartinsriedWest Germany

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