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The dinuclear iron‐oxo ferroxidase center of Pyrococcus furiosus ferritin is a stable prosthetic group with unexpectedly high reduction potentials
Author(s) -
Tatur Jana,
Hagen Wilfred R.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.07.045
Subject(s) - pyrococcus furiosus , chemistry , ferritin , redox , ceruloplasmin , crystallography , dimer , protein subunit , electron paramagnetic resonance , biochemistry , nuclear magnetic resonance , inorganic chemistry , organic chemistry , physics , archaea , gene
Recombinant ferritin from Pyrococcus furiosus expressed in Escherichia coli exhibits in EPR monitored redox titrations a mixed valence (Fe 3+ –Fe 2+ ) S = 1/2 signal at intermediate potentials that is a high‐resolution homolog of the ferroxidase signal previously described for reconstituted horse spleen apo‐ferritin. P. furiosus reconstituted apo‐ferritin reduced to intermediate potentials exhibits the same mixed‐valence signal, which integrates to close to one spin per subunit. The reduction potentials of +210 and +50 mV imply that the iron dimer is a stable prosthetic group with three redox states.