Electron transport via cytochrome C on Si-H surfaces: Roles of Fe and heme

Nadav Amdursky, Israel Pecht, Mordechai Sheves, David Cahen

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


Monolayers of the redox protein Cytochrome C (CytC) can be electrostatically formed on an H-terminated Si substrate, if the protein- and Si-surface are prepared so as to carry opposite charges. With such monolayers we study electron transport (ETp) via CytC, using a solid-state approach with macroscopic electrodes. We have revealed that currents via holo-CytC are almost 3 orders of magnitude higher than via the heme-depleted protein (→ apo-CytC). This large difference in currents is attributed to loss of the proteins' secondary structure upon heme removal. While removal of only the Fe ion (→ porphyrin-CytC) does not significantly change the currents via this protein at room temperature, the 30-335 K temperature dependence suggests opening of a new ETp pathway, which dominates at high temperatures (>285 K). These results suggest that the cofactor plays a major role in determining the ETp pathway(s) within CytC.

Original languageEnglish
Pages (from-to)6300-6306
Number of pages7
JournalJournal of the American Chemical Society
Issue number16
StatePublished - 24 Apr 2013
Externally publishedYes


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