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All the aromatic and most of the methyl group resonances in the 1H NMR spectrum of Cu(I) spinach plastocyanin have been assigned. The binding of the paramagnetic cation Cr(NH3)63+ to the protein has been investigated by both one- and two-dimensional NMR techniques. This relaxation probe causes the broadening of several resonances in the aliphatic region of the spectrum corresponding to spatially separated groups, thus reflecting a large Cr(NH3)63+ -accessible surface. Three groups of negatively charged residues are tentatively assigned as cation binding "sites" on the protein surface. © 1986.

Original publication




Journal article


Journal of Inorganic Biochemistry

Publication Date





171 - 180