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Analysis of Isolated PS I Polypeptides for Acid Labile Sulfide

  • Peter Bordier Høj
  • Barbara Ann Halkier
  • Birger Lindberg Møller

Abstract

Photosystem I (PS I) core particles prepared from a variety of sources all contain the reaction center protein P700-chlorophyll a-protein 1 and a varying number of low molecular weight polypeptides thought to carry one or more of the PS I associated iron-sulfur centres X, A and B. Functional characterization and mapping of these acceptors still remain an enigma, but very recently we have been succesfull in demonstrating the presence of at least one Fe-S centre (most likely centre X (2)) on P700-chlorophyll a-protein 1 (1). Conclusive identification of other PS I polypeptides as Fe-S proteins has not yet been reported although indirect evidence obtained with spinach PS I preparations points towards polypeptides of molecular weight 8 kDa (3) and 19 kDa (4). This paper reports the results on fractionation of full complement PS-I particles into their constituent polypeptides and analysis of their acid labile sulfide content in an attempt to identify additional polypeptides carrying Fe-S centres.

Keywords

Reaction Center Protein Zero Valence Sulfur Constituent Polypeptide Acid Labile Sulfide Preparation Point 
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

© Martinus Nijhoff Publishers, Dordrecht 1987

Authors and Affiliations

  • Peter Bordier Høj
    • 1
  • Barbara Ann Halkier
    • 1
  • Birger Lindberg Møller
    • 1
  1. 1.Department of Plant PhysiologyRoyal Veterinary-and Agricultural UniversityFrederiksberg CDenmark

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