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A Novel Non-heme Iron-binding Ferritin Related to the DNA-binding Proteins of the Dps Family inListeria innocua
1997
Journal of Biological Chemistry
A multimeric protein that behaves functionally as an authentic ferritin has been isolated from the Gram-positive bacterium Listeria innocua. The purified protein has a molecular mass of about 240,000 Da and is composed of a single type of subunit (18,000 Da). L. innocua ferritin is able to oxidize and sequester about 500 iron atoms inside the protein cage. The primary structure reveals a high similarity to the DNA-binding proteins designated Dps. Among the proven ferritins, the most similar
doi:10.1074/jbc.272.6.3259
pmid:9013563
fatcat:bzrsc4pkivhahfga2vjmyyfelm