Abstract
For more than 30 years, continuous wave EPR spectroscopy has been used to characterize active site structures of paramagnetic metalloproteins. For some metal centers, attempts to identity metal ligands from correlative information derived from EPR investigations of model compounds1–5 constitutes some of the earliest examples of how bioinorganic chemistry can be used to mimic physical properties of metal-containing biomolecules.
This work was supported by United State Public Health Service grants RR-02853 and GM-40168
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Peisach, J. (1993). Pulsed EPR Studies of Copper Proteins. In: Karlin, K.D., Tyeklár, Z. (eds) Bioinorganic Chemistry of Copper. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6875-5_2
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