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Nickel superoxide dismutase information


Nickel superoxide dismutase
Structure of Streptomyces Ni superoxide dismutase hexamer[1]
Identifiers
SymbolSod_Ni
PfamPF09055
InterProIPR014123
SCOP21q0d / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 (O
2
) to hydrogen peroxide and molecular oxygen. Superoxide is a reactive oxygen species that is produced in large amounts during photosynthesis and aerobic cellular respiration.[2] 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.[3] Ni-SOD is homohexameric, meaning that it has six identical subunits. Each subunit has a single nickel containing active site.[4] The disproportionation mechanism involves a reduction-oxidation cycle where a single electron transfer is catalyzed by the Ni2+/Ni3+ redox couple.[4][2] Ni-SOD catalyzes close to the barrier of diffusion.

  1. ^ Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K (June 2004). "Crystal structure of nickel-containing superoxide dismutase reveals another type of active site". Proc. Natl. Acad. Sci. U.S.A. 101 (23): 8569–74. Bibcode:2004PNAS..101.8569W. doi:10.1073/pnas.0308514101. PMC 423235. PMID 15173586.
  2. ^ a b Cite error: The named reference pelmenschikov 2006 was invoked but never defined (see the help page).
  3. ^ Zamble, Deborah B.; Li, Yanjie (2009). "Nickel Homeostasis and Nickel Regulation: an Overview". Chemical Reviews. 109 (10): 4617–4643. doi:10.1021/cr900010n. PMID 19711977.
  4. ^ a b Cite error: The named reference J Shearer 2014 was invoked but never defined (see the help page).

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