Association of Fe-S center(s) with the large subunit(s) of photosystem I particles.
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.
D002736:Chloroplasts / Q000502:physiology*; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D007425:Intracellular Membranes / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D008667:Metalloproteins / Q000378:metabolism*; D008970:Molecular Weight; D010788:Photosynthesis; D013440:Sulfides
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D013440:Sulfides