Abstract
X-ray photoelectron spectra were recorded to obtain information regarding the oxidation state of some metallic and non-metallic elements in erythrocuprein. Investigations of various Cu and Zn complexes and salts show marked differences between the binding energies of ionic and complexed bound metals and their ligands. From the intensities of the X-ray photoelectron spectra of the Cu 2p 3 2 and Zn 2p 3 2 levels of erythrocuprein, it can be concluded that Cu is located at the surface of this metalloprotein, whereas Zn must be bound more inside the molecule. X-ray photoelectron spectroscopy promises to be a most valuable new analytical technique for studies on metalloproteins. It is particularly suitable for those metal ions which cannot be detected by electron spin resonance or Mössbauer spectroscopy. In addition to the investigation of metal ions in proteins, other elements, e.g. S present in relatively low concentrations, can be detected.
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