Solid-State electron transport across azurin: From a temperature- independent to a temperature-activated mechanism

Lior Sepunaru, Israel Pecht, Mordechai Sheves, David Cahen

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74 Scopus citations

Abstract

The temperature dependence of current-voltage values of electron transport through proteins integrated into a solid-state junction has been investigated. These measurements were performed from 80 up to 400 K [above the denaturation temperature of azurin (Az)] using Si/Az/Au junctions that we have described previously. The current across the ∼3.5 nm thick Az junction was temperature-independent over the complete range. In marked contrast, for both Zn-substituted and apo-Az (i.e., Cu-depleted Az), thermally activated behavior was observed. These striking temperature-dependence differences are ascribed to the pivotal function of the Cu ion as a redox center in the solid-state electron transport process. Thus, while Cu enabled temperature-independent electron transport, upon its removal the polypeptide was capable only of supporting thermally activated transport.

Original languageEnglish
Pages (from-to)2421-2423
Number of pages3
JournalJournal of the American Chemical Society
Volume133
Issue number8
DOIs
StatePublished - 2 Mar 2011
Externally publishedYes

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