Using scanning electrochemical microscopy (SECM) to measure the electron-transfer kinetics of cytochrome c immobilized on a COOH-terminated alkanethiol monolayer on a gold electrode

Langmuir : the ACS Journal of Surfaces and Colloids
Katherine B Holt

Abstract

Cytochrome c was electrostatically immobilized onto a COOH-terminated alkanethiol self-assembled monolayer (SAM) on a gold electrode at ionic strengths of less than 40 mM. Scanning electrochemical microscopy (SECM) was used to simultaneously measure the electron transfer (ET) kinetics of the bimolecular ET between a solution-based redox mediator and the immobilized protein and the tunneling ET between the protein and the underlying gold electrode. Approach curves were recorded with ferrocyanide as a mediator at different coverages of cytochrome c and at different substrate potentials, allowing the measurement of k(BI) = 2 x 10(8) mol(-1) cm3 s(-1) for the bimolecular ET and k degrees = 15 s(-1) for the tunneling ET. The kinetics of ET was also found to depend on the immobilization conditions of cytochrome c: covalent attachment gave slightly slower tunneling ET values, and a mixed CH3/COOH-terminated ML gave faster tunneling ET rates. This is consistent with previous studies and is believed to be related to the degree of mobility of cyt c in its binding configuration and its orientation with respect to the underlying electrode surface.

References

Jun 29, 2005·Langmuir : the ACS Journal of Surfaces and Colloids·Jelena PetrovićEdmond F Bowden

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Citations

Jan 27, 2012·Chemical Reviews·Francisco Zaera
Mar 14, 2012·Journal of the American Chemical Society·Joaquín Rodríguez-LópezHéctor D Abruña
Jun 22, 2010·Coordination Chemistry Reviews·Amanda L EckermannThomas J Meade
Dec 8, 2017·Analytical and Bioanalytical Chemistry·Javier IzquierdoChristine Kranz
Sep 18, 2007·Biosensors & Bioelectronics·William S RobertsSéamus P J Higson

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