Add time:08/25/2019         Source:sciencedirect.com

Reaction of Cu(II)-stellacyanin with excess (NH3)5Ru(H2O)2+ yields a protein to which (NH3)5Ru(III) is coordinated. The binding stoichiometry of Ru:Cu is (2.1 ± 0.1):1 as shown by ICP atomic emission measurements. In the 1H-NMR spectrum of the Ru(III)-labeled protein, the signals from the C-2H and C-4H protons of His-32 and His-100 are absent. The ESR spectra of the native oxidized Cu(II)-stellacyanin and of the Ru(III)-labeled protein are identical in spite of the (NH3)5Ru(His)3+ ions being a low-spin d5 system. These data are interpreted as being the result of binding of two RU(III) ions to the modified stellacyanin at two proximal imidazole side-chains which are within a separation distance that allows for their electronic coupling.

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