Superoxide Reductase

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{{STRUCTURE_1dqi| PDB=1dqi | SIZE=300| SCENE= |right|CAPTION=Superoxide Reductase tetramer with Fe+3 ion (red), [[1dqi]] }}
{{STRUCTURE_1dqi| PDB=1dqi | SIZE=300| SCENE= |right|CAPTION=Superoxide Reductase tetramer with Fe+3 ion (red), [[1dqi]] }}
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[[Superoxide Reductase]] (SOR) catalyzes the conversion of reduced rubredoxin to rubredoxin using superoxide and H+. The catalysis reaction products are rubredoxin and H<sub>2</sub>O<sub>2</sub>.
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[[Superoxide Reductase]] (SOR) catalyzes the conversion of reduced rubredoxin to rubredoxin using superoxide and H+. The catalysis reaction products are rubredoxin and H<sub>2</sub>O<sub>2</sub><ref>PMID:12072974</ref>.
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[[1y07]] – SOR+Fe(III) – ''Treponema pallidum''<br />
[[1y07]] – SOR+Fe(III) – ''Treponema pallidum''<br />
[[1dqi]], [[1dqk]], [[1do6]] – SOR+Fe(III) – ''Pyrococcus furiosus''<br />
[[1dqi]], [[1dqk]], [[1do6]] – SOR+Fe(III) – ''Pyrococcus furiosus''<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:26, 5 September 2016

Image:2ji1a.png
Crystal Structure of Superoxide Reductase, 2ji1

Template:STRUCTURE 1dqi

Superoxide Reductase (SOR) catalyzes the conversion of reduced rubredoxin to rubredoxin using superoxide and H+. The catalysis reaction products are rubredoxin and H2O2[1].






3D Structures of Superoxide Reductase

Updated on 05-September-2016

2ji1 – DbSOR+Fe(II)+Fe(III) – Desulfovibrio baarsii
2ji2 – DbSOR (mutant)+Fe(II)+Fe(III)
4bff – AfSOR + Fe (II) – Archaeoglobus fulgidus
4c4b, 4c4u – AfSOR (mutant) + Fe (II)
4bgl – AfSOR + Fe (III)
4bfj, 4bfk - AfSOR (mutant)+Fe(III)
2ji3 - DbSOR (mutant)+Fe(III)+peroxide
1vzg, 1vzh, 1vzi - DbSOR (mutant)+Fe(III)+Fe2(CN)6
1y07 – SOR+Fe(III) – Treponema pallidum
1dqi, 1dqk, 1do6 – SOR+Fe(III) – Pyrococcus furiosus

References

  1. ↑ Imlay JA. What biological purpose is served by superoxide reductase? J Biol Inorg Chem. 2002 Jun;7(6):659-63. Epub 2002 Apr 11. PMID:12072974 doi:http://dx.doi.org/10.1007/s00775-002-0361-3

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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