Abstract
Resonance Raman (RR) spectra of type 1 Cu proteins (cupredoxins) show a multiplicity of vibrational fundamentals between 250 and 500 cm-1 that is ascribed to kinematic coupling of the Cu-S(Cys) stretch with deformations of the Cys and His ligand side chains. A similar set of vibrational frequencies is observed for 11 different cupredoxins. These findings suggest that all cupredoxins have a highly conserved Cu(His)2Cys geometry including (i) a trigonal planar array for the three Cu ligands and (ii) a coplanar arrangement of the Cu-S-C ß-Cα-N atoms in the Cu-cysteinate moiety.
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Sanders-Loehr, J. (1993). Investigation of Type 1 Copper Site Geometry by Spectroscopy and Molecular Redesign. In: Karlin, K.D., Tyeklár, Z. (eds) Bioinorganic Chemistry of Copper. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6875-5_4
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DOI: https://doi.org/10.1007/978-94-011-6875-5_4
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