The dinuclear iron-oxo ferroxidase center of Pyrococcus furiosus ferritin is a stable prosthetic group with unexpectedly high reduction potentials |
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Authors: | Tatur Jana Hagen Wilfred R |
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Institution: | Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands. |
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Abstract: | Recombinant ferritin from Pyrococcus furiosus expressed in Escherichia coli exhibits in EPR monitored redox titrations a mixed valence (Fe(3+)-Fe2+) 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. |
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Keywords: | Ferritin Ferroxidase Iron-oxo cluster EPR Redox Pyrococcus furiosus |
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