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EPR Studies of Copper Centers in Proteins

  • Conference paper
Book cover ESR and NMR of Paramagnetic Species in Biological and Related Systems

Part of the book series: Nato Advanced Study Institutes Series ((ASIC,volume 52))

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Abstract

The phenomenological criterion of the fraction of total copper that is detected by EPR classifies copper proteins in three groups, with well defined correlations of EPR properties with their structure and function. Proteins having only EPR-invisible copper contain either Cu(I)—thiolate centers acting in copper-storage or binuclear copper pairs able to bind oxygen. Proteins showing all their copper by EPR have mononuclear copper centers that display distinct EPR parameters, depending on solvent access to the metal site and related to specific protein ligands and mechanisms of electron transfer. The presence of multiple copper centers results in approximately 50% EPR-detectability and in ability to reduce 02 to H20.

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  1. Institute of Biological Chemistry, University of Rome, Rome, Italy

    Giuseppe Rotilio

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  1. Giuseppe Rotilio
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  1. Istituto di Chimica Generale ed Inorganica della, Facoltà di Farmacia, Università di Firenze, Via Gino Capponi, 7 Firenze, Italy

    Ivano Bertini

  2. School of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, Illinois, 61801, USA

    Russell S. Drago

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© 1980 D. Reidel Publishing Company, Dordrecht, Holland

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Rotilio, G. (1980). EPR Studies of Copper Centers in Proteins. 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_14

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