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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 21, Number 6
BKCSDE 21(6)
June 20, 2000 

Effects of Cysteine on the Inactivation of Bovine Liver Catalase
R. Yousefi, A. A. Saboury, M. Ghadermarzi, A. A. Moosavi-Movahedi
Bovine liver catalase was exposed to cysteine, as a natural inactivator metabolize, causing autoxidation-generating H2O2 continuously. The catalase species concentrations and activity measurement were done by spectrophotometry in phosphate buffer 10mM, pH 6.5, and 27 ℃. The activity of catalase decreased continuously due to the conversion of active ferricatalase species, E-Fe (III), to an inactive enzyme species, E-Fe (IV). This conversion is related to the slow production of H2O2 generated by autoxidation of cysteine. The free SH-group of cysteine has an essential role in production of H2O2 and hence inactivation of catalase. NADPH can protect catalase against inactivation due to the conversion of inactive form of E-Fe (IV) to ferricatalase species, E-Fe (Ⅲ)
567 - 570
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