Superoxide dismutase proteins

Klapper, I., Hagstrom, R., Fine, R., Sharp, K., Honig, B. Focusing of electric fields in the active site of cu,zn superoxide dismutase. Proteins Struct. Pune. Genet. 1 (1986) 47-79. 

Durham HD, Roy J, Dong L, Figlewicz DA. Aggregation of mutant Cu/ Zn superoxide dismutase proteins in culture model of ALS. J Neuropathol Exp Neurol 1997 56 523-530. 

Hence, (Cl8TPP)Fe and (Cl8TPP)Mn facihtate the disproportionation of 02, which is equivalent to the function of the iron and manganese superoxide dismutase proteins. 

Urusliitani M, Sik A, Sakui ai T, Nukina N, Takahaslri R, Julien JP (2006) Cln omogranin-mediated secredon of mutant superoxide dismutase proteins linked to amyodoplric lateral sclerosis. Nat Neurosci 9 108—118. 

Kabuta T, Suzuki Y, Wada K (2006) Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by mac-roautophagy and the proleasome. J Biol Chem 281 30524—30533. 

The hypothesis of oxidative damage to striatal neurons mediated by neuroleptic drug enhancement of glutamatergic neurotransmission has been tested in a case-control study (257). Several markers of excitatory neurotransmission (A-acetylaspartylglutamate, A-acety-laspartate, aspartate, and glutamate) and of oxidative damage (superoxide dismutase, protein carbonyl... 

A likely biological function for the superoxide dismutase proteins (SOD) is to remove Oa -, and thereby preclude formation of HOO- [Eq. (5-18)] and prevent initiation of lipid peroxidation and autoxidation (Scheme 5-2). An SOD model... 

Hence, (ClgTPP)Fell (ClgTPP)Mnll facilitate the disproportionation of O2 -, which is equivalent to the function of the iron and manganese superoxide dismutase proteins. Whether the mechanism of Eq. (7-28) is relevant to those for the proteins is unknown, but the absence of electron transfer from their metal centers to O2 - is a reasonable expectation (as is radical-radical coupling of 02"-and the protein in the primary step of the disproportionation mechanism). 

A second belief of most biologists is that the superoxide dismutase proteins safely destroy O2 - via electron-transfer cycles at their transition-metal centers, for example. 

This mechanistic proposal in turn prompts the suggestion that the function of the superoxide dismutase proteins is to prevent free HOO- from coming into contact with allylic C-H bonds in the biological matrix. One approach is to minimize the lifetime of O2 -/HOO-, which is in addition to the radical-radical coupling proposition to deactivate HOO-. For a steady-state flux of 30 X 10 M O2 -/HOO- at pH 5 (1) without superoxide dismutase (SOD) the approximate half-life of O2 -/HOO- is about 30 ms... 

Ceballos, L, Javoy-Agid, F., Delacourte, A., Defossez, A., Lafon, M., Hirsch, E.C., Nicole, A., Sinet, P.M. and Agid, Y. (1991) Neuronal localization of copper-zinc superoxide dismutase protein and mRNA within the human hippocampus from control and Alzheimer s disease brains. Free Radical Res. Commun. 12/13 571-580. 

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. 

Faster longitudinal relaxation and lower RF power (see the succeeding text) paved the way to make faster repetition rates possible ( 500 ms), allowing C— C correlation spectra to be recorded in less than a day on a 1 mg sample of copper zinc superoxide dismutase protein at 60 kHz MAS... 

Holley JA, Janssen YMW, Mossman BT, Taatjes DJ. Increased manganese superoxide dismutase protein in type-II epithelial cells of rat lungs after inhalation of crocidolite asbestos or cristobalite silica. Am J Pathol 1992 141 475-485. 

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