Abstract
Glutathione peroxidase showed an X-ray photoelectron spectroscopy signal of the Se 3d ( 3 2 , 5 2 ) electrons at 54.4 eV. After the addition of the acceptor substrates H 2O 2, a marked shift of this signal to a value of 58.0 eV was observed. Upon subsequent treatment with the donor substrate glutathione, this chemical shift was reversed and the original signal was obtained. These data demonstrate that the enzyme-bound selenium moiety participates in the catalytic process. From the chemical shift obtained it is concluded that the enzyme shuttles between a selenol or selenol derivative in its reduced form and a seleninyl or selenonyl compound in its oxidized form.
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