Probing electron tunneling pathways: Electrochemical study of rat heart cytochrome c and its mutant on pyridine-terminated SAMs
Document Type
Article
Publication Date
10-28-2004
Abstract
The electron-transfer rates between gold electrodes and adsorbed cytochromes are compared for native cytochrome c and its mutant (K13A) using two different immobilization strategies. A recent study by Niki (Niki, K.; Hardy, W. R.; Hill, M. G.; Li, H.; Sprinkle, J. R.; Margoliash, E.; Fujita, K.; Tanimura, R.; Nakamura, N.; Ohno, H.; Richards, J. H.; Gray, H. B. J. Phys. Chem. B 2003, 107, 9947) showed that the electron-transfer rate for a particular mutant cytochrome c (K13A) is orders of magnitude slower than the native form when electrostatically adsorbed on SAM-coated gold electrodes. The current study directly "links" the protein's heme unit to he SAM, thereby "short circuiting" the electron tunneling pathway. These findings demonstrate that the immobilization strategy can modify the electron-transfer rate by changing the tunneling pathway.
Publication Title
Journal of Physical Chemistry B
Recommended Citation
Wei, J.,
Liu, H.,
Niki, K.,
Margoliash, E.,
&
Waldeck, D.
(2004).
Probing electron tunneling pathways: Electrochemical study of rat heart cytochrome c and its mutant on pyridine-terminated SAMs.
Journal of Physical Chemistry B,
108(43), 16912-16917.
http://doi.org/10.1021/jp048148i
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/8094