Methanoferrodoxin represents a new class of superoxide reductase containing an iron-sulfur cluster

Protein MM0632 from the methanogenic archaeon Methanosarcina mazei showed strong superoxide reductase activity and rapidly decomposed superoxide radicals to peroxides. The superoxide reductase activity of the heterologously produced enzyme was determined by a cytochrome c assay and in a test system...

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Bibliographic Details
Published in:The FEBS journal 2011-02, Vol.278 (3), p.442-451
Main Authors: Krätzer, Christian, Welte, Cornelia, Dörner, Katerina, Friedrich, Thorsten, Deppenmeier, Uwe
Format: Article
Language:English
Subjects:
Archaeal Proteins - chemistry
Archaeal Proteins - metabolism
Catalysis
detoxification
Electron Spin Resonance Spectroscopy
Ferredoxins - chemistry
Ferredoxins - metabolism
Iron
Iron-Sulfur Proteins - chemistry
Iron-Sulfur Proteins - metabolism
iron–sulfur protein
methanogenic archaea
Methanosarcina - enzymology
NADP - metabolism
Oxidation
Oxidoreductases - chemistry
Oxidoreductases - metabolism
oxygen radicals
Proteins
Sulfur
superoxide dismutase
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Summary:Protein MM0632 from the methanogenic archaeon Methanosarcina mazei showed strong superoxide reductase activity and rapidly decomposed superoxide radicals to peroxides. The superoxide reductase activity of the heterologously produced enzyme was determined by a cytochrome c assay and in a test system with NADPH, ferredoxin:NADP⁺ reductase, and rubredoxin. Furthermore, EPR spectroscopy showed that MM0632 is the first superoxide reductase that possesses an iron-sulfur cluster instead of a second mononuclear iron center. We propose the name methanoferrodoxin for this new class of superoxide reductase with an [Fe(NHis)₄(SCys)] site as the catalytic center and a [4Fe-4S] cluster as second prosthetic group that is probably involved in electron transfer to the catalytic center. Methanosarcina mazei grows only under anaerobic conditions, but is one of the most aerotolerant methanogens. It is tempting to speculate that methanoferrodoxin contributes to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2010.07964.x