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Metals in Biology pp 91–120Cite as

EPR Studies of Xanthine Oxidoreductase and Other Molybdenum-Containing Hydroxylases

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Part of the book series: Biological Magnetic Resonance ((BIMR,volume 29))

Abstract

A summary is provided both of early work establishing the different types of EPR signals manifested by the molybdenum centers of enzymes such as xanthine oxidoreductase and of more recent studies, frequently employing more advanced EPR-related methods, which have contributed significantly to our understanding of the physical and electronic structures of the enzyme active site. Structures for the signal-giving species, frequently supported by independent x-ray crystallographic studies, are placed in a catalytic context.

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  1. Department of Biochemistry, University of California Riverside, 1463 Boyce Hall, Riverside, CA, 92521-0122, USA

    Russ Hille

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  1. Center for Magnetic Resonance, University of Queensland, St. Lucia, 4072, Australia

    Graeme Hanson

  2. University of Denver, 2190 E. Iliff Avenue,F.W. Olin Hall,Room 202, Denver, 80208-0001, USA

    Lawrence Berliner

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Hille, R. (2010). EPR Studies of Xanthine Oxidoreductase and Other Molybdenum-Containing Hydroxylases. In: Hanson, G., Berliner, L. (eds) Metals in Biology. Biological Magnetic Resonance, vol 29. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-1139-1_5

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