Flavodiiron proteins (FDPs) constitute a large family of enzymes, widespread among the two prokaryotic domains, Bacteria and Archaea, including anaerobes, facultative anaerobes and oxygenic phototrophs. Recently, homologues have also been found in Eukarya, namely algae, mosses and anaerobic protozoa. The distinctive feature of this protein family is a common core built by the fusion of a metallo-β-lactamase-like and flavodoxin-like domains harbouring, respectively, a diiron center and a flavin mononucleotide. These enzymes are endowed with oxygen reductase and/or nitric oxide reductase activities, playing an important role in resistance towards oxidative and/or nitrosative stresses. Cyanobacteria are a particularly interesting example of organisms containing multiple and several unique types of FDPs, whose function appears to be mainly related to protection against oxidative stress conditions, reducing dioxygen to water, and therefore avoiding the formation of reactive oxygen species.
|Title of host publication||Bioenergetic processes of cyanobacteria: from evolutionary singularity to ecological diversity|
|Editors||Günter A. Peschek, Obinger Christian, Renger Gernot|
|Place of Publication||Dordrecht|
|Publication status||Published - 1 Jan 2011|