In Cu-Zn superoxide dismutase

Rosen, D. R., Siddique, T., Patterson, D. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362 59-62, 1993. 

Reaume, A. G., Elliott, J. L., Hoffman, E. K. et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13 43-47,1996. 

Rosen DR, Siddique T, Patterson D, Eiglewicz DA, Sapp P, Hentad A, Donaldson D, Goto J, O Regan JP, Deng HX, et al. (1993) Mutadons in Cu/Zn superoxide dismutase genes are associated widi familial amyotrophic lateral sclerosis. Nature 362 59—62. 

Amino-l-ribosylimidazole-4-carboxamide, cyclization of 78JHC353. Imidazole analogues of nucleic acid components 84MI5. Imidazole-bridged bimetallic center in Cu Zn superoxide dismutase and its... 

Type 2 copper centers are not uniform in ligand or ligand stereochemistries. One common feature is, however, that in the active enzyme, one coordination site is always free to bind oxygen. The most common ligand in type 2 copper centers is histidine. Tyrosine (often modified), methionine, and cysteine occur as well. There are three histidines and a modified tyrosine in amine oxidase and lysyl oxidase [28]. In diamine oxidase, two of the histidine residues have probably been replaced by cysteines [29]. In galactose oxidase, the copper ion is coordinated by two tyrosines, two histidines and an acetate ion [30]. Dopamine-/J-hydroxylase contains two differently coordinated copper ions per functional unit. One is coordinated by three histidines and a methionine and the other by two histidines and another, yet unknown, ligand [ 31 ]. Last but not least, the type 2 copper ion in Cu,Zn-superoxide dismutase is coordinated by four histidine residues, one of which connects the copper ion to the zinc ion, the second metal ion in the active site of the enzyme [32,33] (Fig. 6). 

Deng, H.-X., Hentafi, A., Tainer, J.A., et al. (1993). Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261 1047-1051. 

Falconi, M., Brunelh, M., Pesce, A., Ferrario, M., Bolognesi, M., and Desideri, A. (2003) Static and dynamic water molecules in Cu,Zn superoxide dismutase. Proteins Structure, Function, and Genetics, 51, 607-615. 

Fischer PWF, Campbell JS, Giroux A. 1991. Effects of low copper and high zinc intakes and related changes in Cu,Zn-superoxide dismutase activity on DMBA-induced mammary tumorigenesis. Biological Trace Element Research 30(1) 65-79. 

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