Theoretical Modeling of Enzyme Reaction Chemistry:  The Electron Transfer of the Reduction Mechanism in CuZn Superoxide Dismutase

2004 ◽  
Vol 108 (41) ◽  
pp. 16255-16260 ◽  
Author(s):  
Maira D'Alessandro ◽  
Massimiliano Aschi ◽  
Maurizio Paci ◽  
Alfredo Di Nola ◽  
Andrea Amadei
Keyword(s):  
Electron Transfer ◽  
Superoxide Dismutase ◽  
Enzyme Reaction ◽  
Theoretical Modeling ◽  
Reduction Mechanism ◽  
Cuzn Superoxide Dismutase

scholarly journals Genetically Engineered Polymers of Human CuZn Superoxide Dismutase

1989 ◽  
Vol 264 (9) ◽  
pp. 5260-5268 ◽  
Author(s):  
R A Hallewell ◽  
I Laria ◽  
A Tabrizi ◽  
G Carlin ◽  
E D Getzoff ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Genetically Engineered ◽  
Genetically Engineered Polymers ◽  
Cuzn Superoxide Dismutase

Superoxide radicals mediate the biochemical effects of methylenedioxymethamphetamine (MDMA): Evidence from using CuZn-superoxide dismutase transgenic mice

Synapse ◽  
1995 ◽  
Vol 21 (2) ◽  
pp. 169-176 ◽  
Author(s):  
Jean Lud Cadet ◽  
Bruce Ladenheim ◽  
Hiroshi Hirata ◽  
Richard B. Rothman ◽  
Syed Ali ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Transgenic Mice ◽  
Superoxide Radicals ◽  
Biochemical Effects ◽  
Cuzn Superoxide Dismutase

scholarly journals Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes.

1988 ◽  
Vol 107 (6) ◽  
pp. 2169-2179 ◽  
Author(s):  
L Y Chang ◽  
J W Slot ◽  
H J Geuze ◽  
J D Crapo
Keyword(s):  
Superoxide Dismutase ◽  
Rat Liver ◽  
Oxidant Stress ◽  
Rat Hepatocytes ◽  
Reaction Rates ◽  
Cytoplasmic Matrix ◽  
Cytosolic Proteins ◽  
Cuzn Superoxide Dismutase ◽  
O2 Production

The distribution of CuZn superoxide dismutase (SOD) molecules in subcellular organelles in rat liver hepatocytes was studied using integrated biochemical, stereological, and quantitative immunocytochemical techniques. A known concentration of purified CuZn SOD in 10% gelatin was embedded alongside the liver tissue for the calculation of CuZn SOD concentrations in hepatocyte organelles and total CuZn SOD in the rat liver. Most of the CuZn SOD was located in the cytoplasmic matrix (73.1%) and in the nucleus (11.9%) with concentrations of 1.36 and 0.71 mg/cm3, respectively. Lysosomes contained the highest concentration (5.81 mg/cm3). Only low concentrations were measured in mitochondria (0.21 mg/cm3). Membrane-bound spaces of rough endoplasmic reticulum (ER), smooth ER, and the Golgi system did not contain significant concentrations of the enzyme. By adding up the concentrations in all subcellular compartments, a total liver content of CuZn SOD was established from the immunocytochemical measurements (0.386 +/- 0.028 mg/gm liver) that agreed closely with those obtained by biochemical assays (0.380 +/- 0.058 mg/gm liver). The average distances between two CuZn SOD molecules can be calculated from enzyme concentrations. It was determined that CuZn SOD molecules in the cytoplasmic matrix and nucleus were 34 and 42 nm apart, respectively. In peroxisomes and mitochondria, average intermolecular distance increased to approximately 60 nm and increased to 136 nm in smooth ER. CuZn SOD is a relatively abundant protein in the cytosol of hepatocytes and its distribution overlaps with major sites of O2- production. The efficiency of protection CuZn SOD can provide to cytosolic proteins from attacks by superoxide anion depends on the rate of O2- production, distribution of CuZn SOD relative to cytosolic proteins, and the relative reaction rates between O2- with both cytosolic proteins and CuZn SOD. Future studies of these substrate-enzyme relationships in vivo can lead to a greater understanding of how cells handle oxidant stress.

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