Electron tunneling through Pseudomonas aeruginosa azurins on SAM gold electrodes

Robust voltammetric responses were obtained for wild-type and Y72F/H83Q/Q107H/Y108F azurins adsorbed on CH3(CH2)nSH:HO(CH2)mSH (n = m = 4, 6, 8, 11; n = 13, 15 m = 11) self-assembled-monolayer (SAM) gold electrodes in acidic solution (pH 4.6) at high ionic strengths. Electron-transfer (ET) rates do not vary substantially with ionic strength, suggesting that the SAM methyl headgroup binds to azurin by hydrophobic interactions. The voltammetric responses for both proteins at higher pH values (>4.6–11) also were strong. A binding model in which the SAM hydroxyl headgroup interacts with the Asn47 carboxamide accounts for the relatively strong coupling to the copper center that can be inferred from the ET rates. Of particular interest is the finding that rate constants for electron tunneling through n = 8, 13 SAMs are higher at pH 11 than those at pH 4.6, possibly owing to enhanced coupling of the SAM to Asn47 caused by deprotonation of nearby surface residues.

Robust voltammetric responses were obtained for wild-type and Y72F/H83Q/Q107H/Y108F azurins adsorbed on H3(CH2)nSH:HO(CH2)mSH (n = m = 4, 6, 8, 11; n = 13, 15 m = 11) self-assembled-monolayer (SAM) gold electrodes in acidic solution (pH 4.6) at high ionic strengths. The voltammetric responses for both proteins at higher pH values (>4.6–11) also were strong.Figure optionsDownload as PowerPoint slide