Abstract
The copper containing enzymes superoxide dismutase, dopamine monooxygenase and plasma amine oxidase while functionally diverse are often classified together as ‘non-blue’ or ‘type 2’ on the basis of the similarity of their optical and EPR spectroscopic properties to those of simple mononuclear complexes[1]. X-ray absorption spectroscopy offers a further method of examining the structural relationships within this class of copper proteins. In this paper we summarise the results of EXAFS studies, which provide evidence of structural homologies and have identified imidazole coordination in all three enzyme systems. In the case of native superoxide dismutase where a crystal structure is available to 2Å resolution[2, 3], comparison of EXAFS and crystal lographic coordinates using molecular graphics has provided extra insights into the local structure of the active site.
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Blackburn, N.J., Hasnain, S.S., Knowles, P.F. (1984). EXAFS Studies of Non-Blue Copper Proteins: Superoxide Dimutase, Dopamine-Monooxygenase and Monoamine Oxidase. In: Hodgson, K.O., Hedman, B., Penner-Hahn, J.E. (eds) EXAFS and Near Edge Structure III. Springer Proceedings in Physics, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46522-2_33
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DOI: https://doi.org/10.1007/978-3-642-46522-2_33
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