| Autor: |
Clarke, Michael J., Goodenough, John B., Ibers, James A., Jørgensen, Christian K., Mingos, David Michael P., Neilands, Joe B., Palmer, Graham A., Reinen, Dirk, Sadler, Peter J., Weiss, Raymond, Williams, Robert Joseph P., Gleitzer, C., Goodenough, J. B., Hyde, B. G., O'Keeffe, M., Weser, U., Weser, Ulrich |
| Zdroj: |
Cation Ordering & Electron Transfer; 1985, p145-160, 16p |
| Abstrakt: |
Sulphur containing amino acid residues are found among the structural and functional constituents of many proteins. The ease of oxidising sulphur in these biologically important polymers is well known. At present, there is no simple and fast technique available to monitor the respective oxidation states using chemical reactions. X-ray photoelectron spectroscopy has proven to be both convenient and efficient to follow these electron transport reactions. In the present survey a choice of some sulphur and selenium bearing proteins and metalloproteins will be examined upon excessive irradiation, treatment with hydrogen peroxide and cleavage of metal sulphur bonding. It will also be shown that the use of this technique in general will allow a quick decision on the rate of deterioration of a protein. The limitations of this spectrochemical approach will be debated. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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