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Nickel superoxide dismutase : ウィキペディア英語版 | Nickel superoxide dismutase
Nickel superoxide dismutase (Ni-SOD) is a metalloenzyme that, like the other superoxide dismutases, protects cells from oxidative damage by catalyzing the disproportionation of the cytotoxic superoxide radical (O2-) to hydrogen peroxide and molecular oxygen. Superoxide is a reactive oxygen species that is produced in large amounts during photosynthesis and aerobic cellular respiration.〔 The equation for the disproportionation of superoxide is shown below:
Ni-SOD was first isolated in 1996 from ''Streptomyces'' bacteria and is primarily found in prokaryotic organisms.〔 It has since been observed in cyanobacteria and a number of other aquatic microbes.〔 Ni-SOD is homohexameric, meaning that it has six identical subunits.〔 Each subunit has a single nickel containing active site.〔 The disproportionation mechanism involves a reduction-oxidation cycle where a single electron transfer is catalyzed by the Ni2+/Ni3+ redox couple.〔〔 Ni-SOD catalyzes close to the barrier of diffusion, making it an incredibly efficient enzyme.〔 ==Structure==
Ni-SOD is a globular protein and is shaped like a hollow sphere. It is homohexameric, meaning that it is made up of six identical subunits. Each subunit is a bundle of four right-handed α-helixes and has a molecular mass of 13.4 kDa (117 amino acids). The subunits align to give Ni-SOD a three-fold axis of symmetry.〔 There are six nickel cofactors in total (one for each subunit). The subunits also have a hydrophobic core, which helps drive protein folding. The core is made up of 17 aliphatic amino acids.
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Nickel superoxide dismutase」の詳細全文を読む
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