Superoxide dismutase function

Lehmann Y, Meile L, Teuber M. 1996. Rubrerythrin from Clostridium perfringens cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. J Bacteriol 178 7152-8. 

Cockle, S. A., Bray, R. C. Do all the copper atoms in bovine superoxide dismutase function in catalysis In Superoxide and Superoxide Dismutases (Michelson, A. M., McCord, J, M., Fridovich, L, eds.), London-New York-San Francisco, Academic Press, 1977, pp. 215-216... 

Superoxide dismutase, SOD (54), contains copper and zinc in one subunit. The superoxide anion, 02 , is produced by the reduction of oxygen during respiration in all living species and photosynthesis reactions in plants. This radical anion is toxic probably via the formation of peroxonitrite (54) and hydrogen peroxide (54). Superoxide dismutase functions as an antioxidant via a catalytic reaction (reaction (38)) ... 

Klapper 1, R Hagstrom, RFine, K Sharp and B Honig 1986. Focusing of Electric Fields in tire Actir e Sit of CuZn Superoxide Dismutase Effects of Ionic Strength and Amino-Acid Substitution. Proteins Structure, Function and Genetics 1 47-59. 

CL Eisher, J-L Chen, J Li, D Bashford, L Noodleman. Density-functional and electrostatic calculations for a model of a manganese superoxide dismutase active site in aqueous solution. J Phys Chem 100 13498-13505, 1996. 

McCord, J. M., and Fridovich, I. (1969). Superoxide dismutase an enzymic function for erythrocuprein (hemocuprein)./. Biol. Chem. 244 6049-6055. 

Normally, these reactive species are destroyed by protective enzymes, such as superoxide dismutase in mitochondria and cytosol and catalase in peroxisomes, but if a tissue has been anoxic the respiratory chain is very reduced and reoxygenation allows dangerous amounts to be formed. Muscle also contains significant quantities of the dipeptide, camosine ((J-alanylhistidine) (10—25 mM). The functions of camosine are obscure although it has been suggested to be an effective antioxidant (Pavlov et al., 1993). 

It is possible that dietary flavonoids participate in the regulation of cellular function independent of their antioxidant properties. Other non-antioxidant direct effects reported include inhibition of prooxidant enzymes (xanthine oxidase, NAD(P)H oxidase, lipoxygenases), induction of antioxidant enzymes (superoxide dismutase, gluthathione peroxidase, glutathione S-transferase), and inhibition of redox-sensitive transcription factors. 

Przyklenk, K. and Kloner, R.A. (1986). Superoxide dismutase plus catalase improve contractile function in the canine model of the stunned myocardium. Circ. Res. 58, 148-156. 

Verspaget, H.W., Pena, A.S., Weterman, I.T. and Earners, C.B.H.W. (1988). Diminished neutrophil function in Crohn s disease and ulcerative colitis identified by decreased oxidative metabolism and low superoxide dismutase content. Gut 29, 223-228. 

Gartner, A., and Weser, U. Molecular and Functional Aspects of Superoxide Dismutases. 132, 1-61 (1986). 

Figure 12.2 Copper chaperone function, (a) Copper homeostasis in Enterococcus hirae is affected by the proteins encoded by the cop operon. CopA, Cu1+-import ATPase CopB, Cu1+-export ATPase CopY, Cu1+-responsive repressor copZ, chaperone for Cu1+ delivery to CopY. (b) The CTR family of proteins transports copper into yeast cells. Atxlp delivers copper to the CPx-type ATPases located in the post Golgi apparatus for the maturation of Fet3p. (c) Coxl7p delivers copper to the mitochondrial intermembrane space for incorporation into cytochrome c oxidase (CCO). (d) hCTR, a human homologue of CTR, mediates copper-ion uptake into human cells. CCS delivers copper to cytoplasmic Cu/Zn superoxide dismutase (SOD1). Abbreviations IMM, inner mitochondrial membrane OMM, outer mitochondrial membrane PM, plasma membrane PGV, post Golgi vessel. Reprinted from Harrison et al., 2000. Copyright (2000), with permission from Elsevier Science.

FIGURE 10.6 Comparison of solid-state and liquid-state spectra from a copper protein. The figure illustrates shifts in apparent gz and Az-values of the S = 1/2 and I =3/2 spectrum from Cu11 in bovine superoxide dismutase as a function of the surrounding medium. Top trace frozen aqueous solution at 60 K middle trace frozen water/glycerol (90/10) solution at 60 K bottom trace aqueous solution at room temperature. (Modified from Hagen 1981.)... 

Beauchamp, C.O., Gonias, S.L., Menapace, D.P., and Pizzo, S.V. (1983) A new procedure for the synthesis of polyethylene glycol-protein adducts Effects on function, receptor recognition, and clearance of superoxide dismutase, lactoferrin, and a2macroglobulin. Anal. Biochem. 131, 25-33. 

J.M. McCord, B.B. Keele Jr, and I. Fridovich, Enzyme-based theory of obligate anaerobiosis physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 68, 1024—1027 (1971). 

J.M. McCord and I. Fridovich, Superoxide dismutase. Enzymic function for erythrocuprein (hemo-cuprein). J. Biol. Chem. 244, 6049-6055 (1969). 

M.S. Lah, M.M. Dixon, K.A. Pattridge, W.C. Stallings, J.A. Fee, and M.L. Ludwig, Structure-function in Escherichia coli iron superoxide dismutase comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry. 34, 1646-1660 (1995). 

H.A. Azab, L. Banci, M. Borsari, C. Luchinat, M. Sola, and M.S. Viezzoli, Redox chemistry of superoxide dismutase. Cyclic voltammetry of wild-type enzymes and mutants on functionally relevant residues. Inorg, Chem. 31, 4649-4655 (1992). 

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