Structural studies on cyanobacterial photosystem I |
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Authors: | Myriam Alhadeff Daniel J. Lundell Alexander N. Glazer |
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Affiliation: | (1) Department of Microbiology and Immunobiology, Universityof California, 94720 Berkeley, CA, USA;(2) Present address: Molecular and Cellular Biology, Lawrence Berkeley Laboratory, 94720 Berkeley, CA, USA;(3) Present address: Schering Corporation, 07003 Bloomfield, NJ, USA |
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Abstract: | The cyanobacterial photosystem, I complex from Synechococcus sp. PCC6301 contains polypeptides of apparent Mr of 70,000, 18,000, 17,700, 16,000 and 10,000. Procedures were developed for the purification of the Mr 17,700 and 10,000 polypeptides. Amino acid analyses showed the absence of cystine and cysteine from these polypeptides. Amino-terminal sequences of 98 residues for the Mr 17,700 polypeptide and of 42 residues for the Mr 10,000 polypeptide were determined. Studies of pigment distribution within the photosystem I complex indicated that the binding of chlorophyll a and -carotene is in part dependent on the presence of these polypeptides.Abbreviations PSI photosystem I - P700 reaction center of PSI - SDS sodium dodecylsulfate - TBS tris-buffered saline - TTBS TBS containing Tween-20 |
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Keywords: | Cyanobacteria Photosystem I Polypeptide composition Amino acid sequences /content/l04328u026842207/xxlarge946.gif" alt=" beta" align=" MIDDLE" BORDER=" 0" >-Carotene |
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