Bovine liver catalase was exposed to cysteine, as a natural inactivator met
abolite, causing autoxidation-generating H2O2 continuously. The catalase sp
ecies concentrations and activity measurement were done by spectrophotometr
y in phosphate buffer 10 mM, pH 6.5, and 27 degrees C. The activity of cata
lase decreased continuously due to the conversion of active ferricatalase s
pecies, E-Fe (III), to an inactive enzyme species, E-Fe (IV). This conversi
on is related to the slow production of H2O2 generated by autoxidation of c
ysteine. The free SH-group of cysteine has an essential role in production
of H2O2 and hence inactivation of catalase. NADPH can protect catalase agai
nst inactivation due to the conversion of inactive form of E-Fe (IV) to fer
ricatalase species, E-Fe (III).