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Photosynthesis Research

, Volume 41, Issue 1, pp 105–114 | Cite as

Iron-sulfur centers in the photosynthetic reaction center complex fromChlorobium vibrioforme. Differences from and similarities to the iron-sulfur centers in Photosystem I

  • Bodil Kjær
  • Yean-Sung Jung
  • Lian Yu
  • John H. Golbeck
  • Henrik Vibe Scheller
Group 4: FMO-Protein, Reaction Centers and Electron Transport Regular Papers

Abstract

The photosynthetic reaction center complex from the green sulfur bacteriumChlorobium vibrioforme has been isolated under anaerobic conditions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis reveals polypeptides with apparent molecular masses of 80, 40, 30, 18, 15, and 9 kDa. The 80- and 18-kDa polypeptides are identified as the reaction center polypeptide and the secondary donor cytochromec551 encoded by thepscA andpscC genes, respectively. N-terminal amino acid sequences identify the 40-kDa polypeptide as the bacteriochlorophylla-protein of the baseplate (the Fenna-Matthews-Olson protein) and the 30-kDa polypeptide as the putative 2[4Fe-4S] protein encoded bypscB. Electron paramagnetic resonance (EPR) analysis shows the presence of an iron-sulfur cluster which is irreversibly photoreduced at 9K. Photoaccumulation at higher temperature shows the presence of an additional photoreduced cluster. The EPR spectra of the two iron-sulfur clusters resemble those of FA and FB of Photosystem I, but also show significantly differentg-values, lineshapes, and temperature and power dependencies. We suggest that the two centers are designated Center I (with calculatedg-values of 2.085, 1.898, 1.841), and Center II (with calculatedg-values of 2.083, 1.941, 1.878). The data suggest that Centers I and II are bound to thepscB polypeptide.

Key words

Center I Center II EPR green sulfur bacteria iron-sulfur protein pscB 

Abbreviations

FMO protein

Fenna-Matthews-Olson protein

FWHM

full width half maximum

PS I-A, PS I-B, PS I-C, PS I-D, PS I-E

subunits of Photosystem I

S/N

signal to noise ratio

TMBZ

3,3′,5,5′-tetramethylbenzidine

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Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Bodil Kjær
    • 1
  • Yean-Sung Jung
    • 2
  • Lian Yu
    • 2
  • John H. Golbeck
    • 2
  • Henrik Vibe Scheller
    • 1
  1. 1.Plant Biochemistry Laboratory, Department of Plant BiologyRoyal Veterinary and Agricultural UniversityFrederiksberg C, CopenhagenDenmark
  2. 2.Department of BiochemistryUniversity of NebraskaLincolnUSA

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