Langmuir, Vol.29, No.40, 12511-12519, 2013
Nanoscale Mechano-Electronic Behavior of a Metalloprotein as a Variable of Metal Content
In this work, we have explored an approach to finding a correlation between the mechanical response of a metalloprotein against a range of applied force (by force curve analysis) and its electrical response under pressure stimulation (by current sensing atomic force spectroscopy) at the nanoscale. Iron-storage protein ferritin has been chosen as an experimental model system because it naturally contains a semiconducting iron core. This core consists of a large number of iron atoms and is therefore expected to exert a clear influence on the overall mechanical response of the protein structure. Four different ferritins (apoferritin, Fe(III)-ferritins containing similar to 750 and similar to 1400 iron atoms, and holoferritin containing similar to 2600 iron atoms) were chosen in order to identify any relation between the mechano-electronic behavior of the ferritins and their metal content. We report the measurement of Young's modulus values of the ferritin proteins as applicable in a nanoscale environment, for the first time, and show that these values are directly linked to the iron content of the individual ferritin type. The greater the iron content, the greater the Young's modulus and in general the slower the rate of deformation against the application of force. When compressed, all the four ferritins exhibited increased electronic conductivity. A correlation between the iron content of the ferritins and the current values observed at certain bias voltages could be made at higher bias values (beyond 0.7 V), but no such discrimination among the four compressed ferritins could be made at the lower voltages. We propose that only at higher voltages can the iron atoms that reside deeper inside the core of the ferritins be accessed. The iron atoms that could be situated at the inner wall of the protein shell appear to make a general contribution to the electronic conductivity of the four ferritin systems.