Study Progress of Cu,Zn Superoxide Dismutas——From Gene to Function

VernacularTitle:铜锌超氧化物歧化酶(SOD)研究进展——从基因到功能
Author: Chang-Lu WANG ¹ ; Jun-Wu CAO ; Yu-Rong WANG ; Mian-Hua CHEN ; Zhi-Qiang CHEN ; Shao-Ran TIAN
Author Information

1. 天津科技大学
Keywords: SOD; CuZnSOD; Review
From: Progress in Modern Biomedicine 2008;8(5):940-943
CountryChina
Language:Chinese
Abstract: Superoxide Dismutase (SOD)(EC 1.15.1.1)is a metalloenzyme that is found in almost all organisms and catalyzes the dismutation of superoxide anion radical to hydrogen peroxide and molecular oxygen. Three unique and highly compartmentalized mammalian SOD have been biochemically and molecularly characterized to date: Cu, Zn superoxide dismutase (CuZnSOD, SOD1), MnSOD (Manganese Superoxide Dismutase, SOD2)and EC-SOD (Extracellular Superoxide Dismutase, SOD3). Cu, Zn superoxide dismutase (CuZnSOD, SOD1)is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. CuZnSOD is widely distributed and comprises about 90% of the total SOD. Cytoplasmic and periplasmic SOD exists as dimers,whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes and eukaryotes. CuZnSOD are thought to protect the brain, lungs, and other tissues from oxidative stress. This paper reviewed the gene, molecular and chemical structure and biological function of CuZnSOD.