Association of Fe-S Center(s) with the Large Subunit(s) of Photosystem I Particles1
- 1 July 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 98 (1) , 69-76
- https://doi.org/10.1093/oxfordjournals.jbchem.a135274
Abstract
Treatment of photosystem I particles from spinach (Spinacia oleracea) with dodecyl sulfate destroyed the protein-bound Fe-S centers and converted some of the acid-labile sulfide to zero-valence sulfur which remained covalently bound to the proteins. When the proteins were resolved by gel-permeation chromatography or by polyacrylamide gel electrophoresis in the presence of dodecyl sulfate, a considerable amount of zero-valence sulfur was associated with the large molecular weight polypeptide(s) (63,000 and 59,000). The results strongly suggest that an intact two peptide P700 chlorophyll a-protein is an Fe-S protein.Keywords
This publication has 1 reference indexed in Scilit:
- Isolation and characterization of a subchloroplast particle enriched in iron-sulfur protein and P700Archives of Biochemistry and Biophysics, 1977