Impact of surface immobilization and solution ionic strength on the formal potential of immobilized cytochrome C.
Four different self-assembled monolayer (SAM) electrode systems were examined electrochemically in order to better understand surface charge effects on the redox thermodynamics of immobilized horse heart cytochrome c (cyt c). Neutralization of protein surface charge upon adsorption on anionic COOH-terminated SAMs was found to cause substantial changes in the formal potential, as determined by cyclic voltammetry. For cyt c immobilized on negatively charged surfaces, the formal potential shifted to more negative values as the ionic strength was decreased, which is opposite to the trend displayed by solution cyt c. In contrast, immobilization to uncharged interfaces resulted in an ionic strength dependence for cyt c that is similar to its solution behavior. The results provide insight into the importance of surface charge on the formal potential of cyt c.
Petrović
Jelena
J
Department of Chemistry, Mathematics and Physical Sciences, Saint Francis University, Loretto, Pennsylvania 15940, USA.
Clark
Rose A
RA
Yue
Hongjun
H
Waldeck
David H
DH
Bowden
Edmond F
EF
D000327:Adsorption; D045304:Cytochromes c / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D009994:Osmolar Concentration; D012996:Solutions; D055672:Static Electricity
D004800:Enzymes, Immobilized; D012996:Solutions; D045304:Cytochromes c