Force dependent metalloprotein conductance by conducting atomic force microscopy

Our ability to analyse charge transport through a biological macromolecule, pertinent to our understanding not only of biological redox processes but also, for example, to our interpretation of tunnelling imaging, remains a significant practical and theoretical issue. Though much information can be gained by carrying out such examinations at a molecular level, there exist few methods where such controlled analyses are, in fact, feasible. Here we report on the electron transport characteristics of a blue copper metalloprotein as characterized at a refined level by conductive-probe atomic force microscopy. The modulation of this conductance with compressional force has also been examined. Though highly resistive, observations are consistent with the ability of the protein matrix to mediate appreciable tunnelling current. This work, then, paves the way for designed implementation of biomacromolecules into electronic devices.