Weak, noncovalent interactions (dipoledipole interactions, hydrogen bonding, and Van der Waals forces) in ligand-receptor pairs play a very important role in living systems. A new way to study these interactions is by using electron transfer theory. The rate of electron transfer between redox centers is dependent on several factors, including reorganization energy, which incorporates these weak interactions. Binding of a protein receptor to a redox-modified ligand will change the reorganization energy of a system. Thus, the rate of electron transfer can be measured using electrochemical techniques. A molecule was designed to incorporate a ligand (desthiobiotin), a metal complex (ruthenium pentaammine), and an alkane thiol. The molecule was synthesized and characterized, and there was an attempt made to incorporate the redox-modified ligand into self-assembled monolayers on gold electrodes. The potentials and the rates of electron transfer of this system were measured in the presence and absence of avidin, a tetrameric protein. From the electrochemical data gathered thus far, it was impossible to conclude whether or not avidin affects the rate of electron transfer. 

Last modified

• 07/18/2018

Creator

• Amanda Eckermann
• Thomas Meade
• Tracy Ooi

DOI

• https://doi.org/10.21985/N2H70K

Keyword

• Volume 4

Date created

• 2007

Resource type

• Article

Rights statement

• In Copyright