TY - JOUR
T1 - Reactions of hypochlorite with catalase
AU - Mashino, Tadahiko
AU - Fridovich, Irwin
N1 - Funding Information:
This work was supported by research grants from the United States Army Research Office, the Council for Tobacco Research, U.S.A., Inc., the National Science Foundation, and the Institute of General Medical Sciences of the National Institutes of Health.
PY - 1988/8/31
Y1 - 1988/8/31
N2 - OCl-/HOCl imposed a rapid inactivation of catalase (hydrogen-peroxide: hydrogen-peroxide oxidoreductase, EC 1.11.1.6), some of which was slowly reversible upon subsequent exposure to H2O2. Ethanol accelerated this restoration of activity by H2O2. OCl- caused biphasic changes in the visible absorption spectrum of catalase, which were partially reversed by dithionite. A scheme of reactions involving axial ligation of one or two OCl- to heme iron, followed by heterolytic or homolytic cleavages of the OCl bond, is proposed to account for the behavior of the system.
AB - OCl-/HOCl imposed a rapid inactivation of catalase (hydrogen-peroxide: hydrogen-peroxide oxidoreductase, EC 1.11.1.6), some of which was slowly reversible upon subsequent exposure to H2O2. Ethanol accelerated this restoration of activity by H2O2. OCl- caused biphasic changes in the visible absorption spectrum of catalase, which were partially reversed by dithionite. A scheme of reactions involving axial ligation of one or two OCl- to heme iron, followed by heterolytic or homolytic cleavages of the OCl bond, is proposed to account for the behavior of the system.
KW - Catalase
KW - Hypochlorous acid
KW - Sodium hypochlorite
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U2 - 10.1016/0167-4838(88)90298-1
DO - 10.1016/0167-4838(88)90298-1
M3 - Article
C2 - 2841981
AN - SCOPUS:0023678592
SN - 1570-9639
VL - 956
SP - 63
EP - 69
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 1
ER -