View source for Ceci 2011 Extremophiles

{{Publication
|title=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E (2011) The characterization of ''Thermotoga maritima'' ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress. Extremophiles 15:431-9.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21487935 PMID: 21487935]
|authors=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E
|year=2011
|journal=Extremophiles
|abstract=Ferritin from the hyperthermophilic anaerobe ''Thermotoga maritima'', a bacterium of ancient phylogenetic origin, is structurally similar to known bacterial and eukaryotic ferritins: 24 identical subunits assemble into a shell having octahedral symmetry and a Mr of about 460 kDa. ''T. maritima'' ferritin (TmFtn), purified to homogeneity as a recombinant protein, contains approximately 2-3 iron atoms and can incorporate efficiently up to 3,500 atoms in the form of a ferric oxy-hydroxide mineral at 80 °C, the optimal growth temperature of the bacterium. The 24-mer unexpectedly dissociates reversibly into dimers at low ionic strengths. In turn, dimers re-associate into the native 24-mer assembly at high protein concentrations and upon incorporation of iron micelles containing at least 500 Fe(III). TmFtn uses O<sub>2</sub> as efficient iron oxidant. The reaction stoichiometry is 3-4 O<sub>2</sub>:Fe(II) as in all bacterial ferritins. Accordingly no H<sub>2</sub>O<sub>2</sub> is released into solution, a feature reflected in the in vitro ability of TmFtn to reduce significantly iron-mediated oxidative damage to DNA at 80 °C. A similar TmFtn-mediated ROS detoxifying role likely occurs in the bacterium which lacks the SOD/catalase defense systems of the aerobic world.
|keywords=Thermotoga maritima ferritin, Subunit association-dissociation properties, Iron incorporation, DNA protection, ROS detoxification
}}
{{Labeling
|organism=Rat, Eubacteria
|preparations=Enzyme
|instruments=Oxygraph-2k
}}