X-ray photoelectron spectra of iron-sulphur proteins.
The X-ray photoelectron spectra of the 2p, 3s and 3p levels of iron in oxidized Clostridium pasteurianum ferredoxin indicate that the eight iron atoms in the molecule are indistinguishable. Their magnetic state is indicated both by core polarization splitting of the 3s electrons, and by "shake-up' satellites on the 2p lines. Similar satellites are observed in the 2p lines of reduced Chromatium high-potential iron-sulphur proteins and oxidized spinach ferredoxin, indicating that there too the iron atoms are magnetic. The low observed magnetic susceptibility of these proteins is therefore due to spin-coupling between the iron atoms in the active centre.
D002844:Chromatium / Q000032:analysis; D003013:Clostridium / Q000032:analysis; D005288:Ferredoxins / Q000032:analysis; D007501:Iron / Q000032:analysis; D008667:Metalloproteins / Q000032:analysis; D010084:Oxidation-Reduction; D010944:Plants / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D013057:Spectrum Analysis; D013455:Sulfur / Q000032:analysis; D014965:X-Rays
D005288:Ferredoxins; D008667:Metalloproteins; D013455:Sulfur; D007501:Iron