THE ACTIVE CENTER OF BACTERIAL CATALASE INVESTIGATED BY MÖSSBAUER SPECTROSCOPY
Domain: Physics
57Fe enriched bacterial catalase obtained from Micrococcus luteus was investigated by Mössbauer spectroscopy. At pH 6.3 in an acetate buffer the Mössbauer spectra are very similar to the spectra of metmyoglobin, indicating a similar level scheme of the iron. A least squares fit of a spectrum at 4.2 K with an applied field Hext= 0.5 kOe yielded g-values which agree well with EPR-measurements. The four subunits of the catalase behaved identically. In a sample with phosphate buffer at pH 7.0 we found a second iron species, which may come from a denaturation process or a conformational change.
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57Fe enriched bacterial catalase obtained from Micrococcus luteus was investigated by Mössbauer spectroscopy. At pH 6.3 in an acetate buffer the Mössbauer spectra are very similar to the spectra of metmyoglobin, indicating a similar level scheme of the iron. A least squares fit of a spectrum at 4.2 K with an applied field Hext= 0.5 kOe yielded g-values which agree well with EPR-measurements. The four subunits of the catalase behaved identically. In a sample with phosphate buffer at pH 7.0 we found a second iron species, which may come from a denaturation process or a conformational change.
Article published online by
EDP Sciences
and available at
http://dx.doi.org/10.1051/jphyscol:19792183
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Publié le :
29/06/2012
Langue :
Français
Nombre de pages :
3
Type de la publication :
Rapports et thèses
Thème :
Savoirs >
Science de la nature
Source :
Journal de Physique Colloques
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