Abstract
Bovine erithrocyte copper-zinc superoxide dismutase Cu(11)-Zn(11)SOD is a dimer made of two equivalent subunits each containing one copper and one zinc atom. X-ray diffraction study (1) on crystals of native Cu,Zn SOD have shown the copper to be coordinated to four histidines (His 44, His 46, His 61 and His 118) and one molecule of water. One of the histidines (His 61) provides an imidazolate bridge between the copper and the zinc.
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© 1987 Springer-Verlag Berlin Heidelberg
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Desideri, A., Morante, S., Rotilio, G. (1987). The Active Site of Cu,Zn Superoxide Dismutase as Studied by EXAFS: The Binding of Chloride to the Reduced Enzyme. In: Bianconi, A., Congiu Castellano, A. (eds) Biophysics and Synchrotron Radiation. Springer Series in Biophysics, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71490-0_19
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DOI: https://doi.org/10.1007/978-3-642-71490-0_19
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