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• W2061736316 abstract "Oxidative stress is a universal phenomenon experienced by organisms in all domains of life. Proteins like those in the ferritin-like di-iron carboxylate superfamily have evolved to manage this stress. Here we describe the cloning, isolation, and characterization of a Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (PfDps-like). Phylogenetic analysis, primary structure alignments and higher order structural predictions all suggest that the P. furiosus protein is related to proteins within the broad superfamily of ferritin-like di-iron carboxylate proteins. The recombinant PfDps protein self-assembles into a 12 subunit quaternary structure with an outer shell diameter of ∼10 nm and an interior diameter of ∼5 nm. Dps proteins functionally manage the toxicity of oxidative stress by sequestering intracellular ferrous iron and using it to reduce H2O2 in a two electron process to form water. The iron is converted to a benign form as Fe(III) within the protein cage. This Dps-mediated reduction of hydrogen peroxide, coupled with the protein’s capacity to sequester iron, contributes to its service as a multifunctional antioxidant." @default.
• W2061736316 created "2016-06-24" @default.
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• W2061736316 date "2006-05-01" @default.
• W2061736316 modified "2023-10-11" @default.
• W2061736316 title "Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus" @default.
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• W2061736316 doi "https://doi.org/10.1016/j.jinorgbio.2005.12.001" @default.
• W2061736316 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16412514" @default.
• W2061736316 hasPublicationYear "2006" @default.
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