Copper/zinc superoxide dismutase

Copper-zinc-superoxide dismutase (from blood cell haemolysis) [9054-89-1J Mr 32,000... 

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Richardson, J.S., et al. Similarity of three-dimensional stmcture between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit. 

Tainer, J.A., et al. Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase. 

Structure and Properties of Copper-Zinc Superoxide Dismutases Ivano Bertini, Stefano Mangani, and Maria Silvia Viezzoli... 

Ceballos-Picot, I., Nicole, A., Briand, P., Grimber, G., Delacourte, A., Defossez, A., Javoy-Agid, F., Lafon, M., Blouin, J.L. and Sinet, P.M. (1991). Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice animal model of gene dosage effects in Down s syndrome. Brain Res, 552, 198-214. 

Phase II trial of copper zinc superoxide dismutase (CuZnSOD) in treatment of Crohn s disease. Free Rad. Biol. Med. 7, 145-149. 

Kulkami-Narla A., Getchell T.V. and Getchell M.L. (1997). Differential expression of manganese and copper-zinc superoxide dismutases in the olfactory and vomeronasal receptor neurons of rats during ontogeny. J Comp Neurol 381, 31-40. 

Y. Tian, M. Shioda, S. Kasahara, T. Okajima, F. Mao, T. Hisabori, and T. Ohsaka, A facilitated electron transfer of copper-zinc superoxide dismutase (SOD) based on a cysteine-bridged SOD electrode. Biochim. Biophys. Acta. 1569, 151-158 (2002). 

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Z. Wang, W. Qian, Q. Luo, and M. Shen, Abnormal electrochemical behavior of copper-zinc superoxide dismutase on mercury electrodes. J. Electroanal. Chem. 482, 87-91 (2000). 

M.W. Pantoliano, P.J. McDonnell, and J.S. Valentine, Reversible loss of metal ions from the zinc binding site of copper-zinc superoxide dismutase. The low pH transition. J. Amer. Chem. Soc. 101, 6454— 6456 (1979). 

Y. Tian, T. Ariga, N. Takashima, T. Okajima, L. Mao, and T. Ohsaka, Self-assembled monolayers suitable for electron-transfer promotion of copper, zinc-superoxide dismutase. Electrochem. Commun. 6, 609-614 (2004). 

J.A. Fee, The copper/zinc superoxide dismutase. Ions Biol. Syst. 13, 259—298 (1981). 

Pasinelli, P., Borchelt, D. R., Houseweart, M. K., Cleveland, D. W. and Brown, R. H. Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase. Neurobiology 95 15763-15768,1998. 

Copper is part of several essential enzymes including tyrosinase (melanin production), dopamine beta-hydroxylase (catecholamine production), copper-zinc superoxide dismutase (free radical detoxification), and cytochrome oxidase and ceruloplasmin (iron conversion) (Aaseth and Norseth 1986). All terrestrial animals contain copper as a constituent of cytochrome c oxidase, monophenol oxidase, plasma monoamine oxidase, and copper protein complexes (Schroeder et al. 1966). Excess copper causes a variety of toxic effects, including altered permeability of cellular membranes. The primary target for free cupric ions in the cellular membranes are thiol groups that reduce cupric (Cu+2) to cuprous (Cu+1) upon simultaneous oxidation to disulfides in the membrane. Cuprous ions are reoxidized to Cu+2 in the presence of molecular oxygen molecular oxygen is thereby converted to the toxic superoxide radical O2, which induces lipoperoxidation (Aaseth and Norseth 1986). 

The transfer of a quadridentate N2S2-donor ligand from M2+ (M = Cr, Mn, Fe, Co or Ni) to Cu2+ (271), already mentioned in Section V.A.l, has a formal connection with an investigation of the mechanism of copper delivery to metalloproteins, such as copper zinc superoxide dismutase. Both are ligand exchange reactions of the type ML + CuL ML + CuL (300). 

Potter, S.Z. and Valentine, J.S. (2003) The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig s disease), J. Biol. Inorg. Chem., 8, 373-380. 

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