期刊
FEBS LETTERS
卷 579, 期 21, 页码 4729-4732出版社
WILEY
DOI: 10.1016/j.febslet.2005.07.045
关键词
ferritin; ferroxidase; iron-oxo cluster; EPR; redox; Pyrococcus furiosus
Recombinant ferritin from Pyrococcus furiosus expressed in Escherichia coli exhibits in EPR monitored redox titrations a mixed valence (Fe3+-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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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