Yokoyama, K. and Nakamura, N. and Ohno, H. and Winkler, J. R. and Richards, J. H. and Gray, H. B. (2010) Electron tunneling through mutant azurins on mixed SAM gold electrodes. In: International Chemical Congress of Pacific Basin Societies (Pacifichem 2010), December 15-20, 2010, Honolulu, HI. http://resolver.caltech.edu/CaltechAUTHORS:20120816-072045664
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We are investigating interfacial electron transfer rates of P. aeruginosa azurin and its mutants using electrochem. at 1:1 CH3(CH2)nSH:HO(CH2)nSH mixed-SAM gold electrodes. We have examd. interfacial electron transfer rates of mutant azurins in which asparagine-47 was replaced by alanine, aspartic acid, lysine, arginine, leucine, threonine, serine, and glutamine. The N47D mutant on a mixed SAM exhibited a well-defined electrochem. response; N47T and N47S gave a weak signal; but the other 5 mutants showed no response. It is likely that the N47 side-chain carbonyl interacts with the mixed SAM surface, providing a very favorable electron tunneling pathway to the copper via an N47-C112 hydrogen bond. We also have examd. interfacial electron transfer rates of M121X mutant azurins. The ET rates for M121E are 2 orders of magnitude smaller; those for M121Q are almost 1 order of magnitude smaller; and those for the M121L protein are similar to those of wild-type azurin at pH 7. In addn., we have found that type zero azurins have higher ET rates than those of type 2 proteins (rates for C112D are 3 orders of magnitude smaller; those for type zero C112D/M121X (X=L and I) are 2 orders of magnitude smaller than wild-type at pH 7).
|Item Type:||Conference or Workshop Item (Paper)|
|Additional Information:||© 2012 American Chemical Society.|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||16 Aug 2012 18:49|
|Last Modified:||23 Aug 2016 10:16|
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