作者: Joan Selverstone Valentine , Lisa M. Ellerby , Janet A. Graden , Clinton R. Nishida , Edith Butler Gralla
DOI: 10.1007/978-94-011-0255-1_8
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摘要: Copper-zinc superoxide dismutase (CuZnSOD) is one of a class enzymes known to be excellent catalysts the disproportionation (2 O 2 - + H+ → O2 H2O2). An unusual aspect structure this enzyme occurrence bridging imidazolate ligand, which holds copper and zinc ions in each subunit 6.3 A apart. The mechanism CuZnSOD-catalyzed understood broad outline, but only relatively recently has it been possible address several important aspects structure-function relationships enzyme. Of particular interest are pH independence both spectroscopic catalytic properties over wide range function zinc-imidazolate ligand mechanism. Recently, there have intriguing results concerning physiological role played by CuZnSOD vivo. There growing body evidence indicating that oxidative damage mammalian cells associated with aging, carcinogenesis, induction other serious disease states toxic metabolites derived from metabolism may responsible for such damage. Superoxide dismutases proposed act as antioxidant lowering steady state concentration Mutations also reported familial form amyotrophic lateral sclerosis (ALS), frequently termed Lou Gehrig’s Disease, these mutations cause yet unknown.