Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
