Multiple actions of superoxide dismutase: why can it both inhibit and stimulate reduction of oxygen by hydroquinones?
Superoxide dismutase can either inhibit or stimulate autoxidation of different hydroquinones, suggesting multiple roles for O2.-. Inhibitory actions of superoxide dismutase include termination of O2.(-)-propagated reaction chains and metal chelation by the apoprotein. Together, chelation of metals and termination of O2.(-)-propagated chains can effectively prevent reduction of oxygen. Chain termination by superoxide dismutase can thus account for negligible accumulation of H2O2 without invoking a superoxide:semiquinone oxidoreductase activity for this enzyme. One stimulatory action of superoxide dismutase is to decrease thermodynamic limitations to reduction of oxygen. Whether superoxide dismutase inhibits or accelerates an autoxidation depends on the reduction potentials of the quinone and the availability of metal coordination for inner sphere electron transfers.
Bandy
B
B
Bioenergetics Research Laboratory, Faculty of Applied Sciences, School of Kinesiology, Simon Fraser University, Burnaby, B.C.
Moon
J
J
Davison
A J
AJ
D000818:Animals; D002614:Chelating Agents; D004357:Drug Synergism; D005609:Free Radicals; D006873:Hydroquinones / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000494:pharmacology*; D013816:Thermodynamics
D002614:Chelating Agents; D005609:Free Radicals; D006873:Hydroquinones; D013482:Superoxide Dismutase; D010100:Oxygen; C031927:hydroquinone