Probing Electron Tunneling Pathways: Electrochemical Study of Rat Heart Cytochromecand Its Mutant on Pyridine-Terminated SAMs

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 the 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.

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