Abstract
This article discusses some correlations between electron paramagnetic resonance and Mössbauer spectroscopy which can be utilized to unravel some of the complexities of proteins containing many metal atoms. After describing the qualitative features of Mössbauer spectra observed for Kramers and non-Kramers systems recent findings on the MoFe protein of nitro-genase (the biological nitrogen fixing system) will be discussed. Mössbauer and EPR studies of the MoFe protein (30 Fe atoms) have lead to a detailed spectroscopic characterization of two novel spin-coupled metal centers.
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© 1980 D. Reidel Publishing Company, Dordrecht, Holland
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Münck, E., Huynh, B.H. (1980). Iron-Sulfur Proteins: Combined Mössbauer and EPR Studies. In: Bertini, I., Drago, R.S. (eds) ESR and NMR of Paramagnetic Species in Biological and Related Systems. Nato Advanced Study Institutes Series, vol 52. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-9524-6_12
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DOI: https://doi.org/10.1007/978-94-009-9524-6_12
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