Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Holt, K.B.

Holt,

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.

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) cm(3) 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 CH(3)/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.[1]

References

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. Holt, K.B. Langmuir : the ACS journal of surfaces and colloids. (2006) [Pubmed]

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