TY - JOUR
T1 - Independent activity of catalase haematins
AU - Kremer, Mordechai L.
PY - 1970/12
Y1 - 1970/12
N2 - The peroxidatic mechanism for the catalytic reaction and for peroxidation has been extended from haematin basis to include the catalase molecule as a whole. It has been shown that interaction among single haematin units does not affect the form of the rate equations for the catalatic reaction. An analysis of the kinetics of the competition of the catalatic and peroxidatic reactions shows, however, that catalase haematins are equivalent and non-interacting during catalysis. The implication of this result in relation to the catalysis by catalase subunits is discussed.
AB - The peroxidatic mechanism for the catalytic reaction and for peroxidation has been extended from haematin basis to include the catalase molecule as a whole. It has been shown that interaction among single haematin units does not affect the form of the rate equations for the catalatic reaction. An analysis of the kinetics of the competition of the catalatic and peroxidatic reactions shows, however, that catalase haematins are equivalent and non-interacting during catalysis. The implication of this result in relation to the catalysis by catalase subunits is discussed.
UR - http://www.scopus.com/inward/record.url?scp=0014908748&partnerID=8YFLogxK
U2 - 10.1016/0022-5193(70)90104-9
DO - 10.1016/0022-5193(70)90104-9
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C2 - 5492993
AN - SCOPUS:0014908748
SN - 0022-5193
VL - 29
SP - 387
EP - 394
JO - Journal of Theoretical Biology
JF - Journal of Theoretical Biology
IS - 3
ER -