Abstract
The MoFe-protein (component 1) of nitrogenase contains two major classes of metal clusters, called P and M. In the as-isolated form of the protein, the P-clusters are diamagnetic while the M-centers are paramagnetic, yielding an EPR spectrum of an S=3/2 species. This protein was titrated with thionin to oxidize the P-clusters, converting them into paramagnetic species while preserving the paramagnetism of the M-centers. During this titration, the relaxation properties of the protein's M-centers were monitored with an EPR spectrometer using the technique of progressive power saturation
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