Copper-Zinc Superoxide Dismutase: Mechanistic and Biological Studies

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

关键词:

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.

参考文章(38)
H E Parge, E D Getzoff, C S Scandella, R A Hallewell, J A Tainer, Crystallographic characterization of recombinant human CuZn superoxide dismutase Journal of Biological Chemistry. ,vol. 261, pp. 16215- 16218 ,(1986) , 10.1016/S0021-9258(18)66701-8
Bioinorganic chemistry of copper Springer-Science+Business Media. ,(1993) , 10.1007/978-94-011-6875-5
June S. Taylor, Joseph E. Coleman, Electron spin resonance of metallocarbonic anhydrases. Journal of Biological Chemistry. ,vol. 246, pp. 7058- 7067 ,(1971) , 10.1016/S0021-9258(19)45949-8
Edith Butler Gralla, Daniel J. Kosman, Molecular genetics of superoxide dismutases in yeasts and related fungi. Advances in Genetics. ,vol. 30, pp. 251- 319 ,(1992) , 10.1016/S0065-2660(08)60322-3
I Fridovich, Superoxide dismutases: an adaptation to a paramagnetic gas Journal of Biological Chemistry. ,vol. 264, pp. 7761- 7764 ,(1989) , 10.1016/S0021-9258(18)83102-7
Lucia BANCI, Ivano BERTINI, Diane E. CABELLI, Robert A. HALLEWELL, James W. TUNG, Maria Silvia VIEZZOLI, A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins. FEBS Journal. ,vol. 196, pp. 123- 128 ,(1991) , 10.1111/J.1432-1033.1991.TB15794.X
K. T. Tamai, E. B. Gralla, L. M. Ellerby, J. S. Valentine, D. J. Thiele, Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase Proceedings of the National Academy of Sciences of the United States of America. ,vol. 90, pp. 8013- 8017 ,(1993) , 10.1073/PNAS.90.17.8013
Elizabeth D. Getzoff, John A. Tainer, Paul K. Weiner, Peter A. Kollman, Jane S. Richardson, David C. Richardson, Electrostatic recognition between superoxide and copper, zinc superoxide dismutase Nature. ,vol. 306, pp. 287- 290 ,(1983) , 10.1038/306287A0