Ruthenium(II) Polypyridine Complexes and the Electron-Transfer Reactions of Metalloproteins

• Bill Durham ^[1] ; Frank Millett ^[1]
  1. [1] Department of Chemistry and Biochemistry, University of Arkansas
• Localización: Journal of chemical education, ISSN 0021-9584, Vol. 74, Nº 6 (June), 1997, págs. 636-640
• Idioma: inglés
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• Resumen

  • Over the past decade, a variety of ruthenium complexes have been used to study electron-transfer reactions in metalloproteins. In the majority of these studies, the ruthenium complexes provide a means of photochemically initiating a rapid electron-transfer reaction. These reactions can be used in several different schemes to: 1) probe structural features which determine the magnitude of the electronic coupling between redox centers in metalloproteins, 2) measure the rate constants for electron transfer between two metalloproteins, 3) investigate the binding interactions between two proteins and 4) measure the rate constants for formation and dissociation of protein-protein complexes. The basic reactions involved in the photochemical schemes and the covalent binding of ruthenium complexes to metalloproteins are described. Several examples involving cytochrome c and cytochrome b5 are used to illustrate the methodology.