Ruthenium-modified proteins. Reactions of cis-[ Ru(NH3)4(OH2)2]2+ and cis-[ Ru(en)2(OH2)2]2+ with azurin,myoglobin and cytochrome c |
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| Affiliation: | 1. Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, Portugal;2. Gecco Biotech, Nijenborgh 4, Groningen 9747AG, the Netherlands |
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| Abstract: | Reactions of cis-[Ru(en)2(OH2)2]2+ (or cis-[Ru (NH3)4(OH2)2]2+) with Pseudomonas aeruginosa azurin (Az), horse heart myoglobin (Mbh), and horse heart cytochrome c (cyt c) give Ru-labelled proteins. The ruthenium binding sites in the singly modified derivatives are His-83 (Az), His-81 (Mbh), and His-33 (cyt c). Spectroscopic and electrochemical measurements indicate that the structures of the proteins are not perturbed by the surface-bound ruthenium complexes. The E°f values of the Ru(III)/(II) couple in these Ru-modified proteins fall between −0.07 and −0.13 V vs. NHE. |
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