Laccase, a multicopper oxidase, catalyses the four electron reduction of oxygen to water. Upon adsorption to an electrode surface, laccase is known to reduce oxygen at overpotentials lower than the best noble metal electrocatalysts usually employed. While the electrocatalytic activity of laccase is well established on carbon electrodes, laccase does not typically adsorb to better defined noble metal surfaces in an orientation that allows for efficient electrocatalysis. In this work, we utilized anthracene-2-methanethiol (AMT) to modify the surface of Au electrodes and examined the electrocatalytic activity of adsorbed laccase. AMT facilitated the adsorption of laccase, and the onset of electrocatalytic oxygen reduction was observed as high as 1.13 VRHE. We observed linear Tafel behavior with a 144 mV/dec slope, consistent with an outer sphere single electron transfer from the electrode to a Cu site in the enzyme as the rate determining step of the oxygen reduction mechanism.

We compare the association of an ortho-substituted and a planar PCB (polychlorinated biphenyls PCB-52 and PCB-77, respectively) with single-component phospholipid bilayers terminated with phosphocholine headgroups. First, fluorescence correlation spectroscopy (FCS) studies of diffusion on supported fluid-phase DLPC show that the ortho-substituted PCB diffuses more slowly, indicating either complex formation or obstructed diffusion. Differential scanning calorimetry (DSC) of vesicles formed from DMPC shows that the gel-to-fluid phase transition temperature is lower for vesicles containing this ortho-substituted PCB. Atomic force microscopy (AFM) shows that, whereas supported bilayers of DMPC containing this ortho-substituted PCB display two melting points, bilayers containing the coplanar PCB display just a single melting point. A model is proposed in which the ortho-substituted PCB resides within the lipid tails of these phospholipid bilayers but the coplanar PCB associates preferentially with the headgroups. This model is consistent with the known membrane disruptive ability of the ortho substituted isomer.

In their comment, Jonker and van der Heijden (1) agree with us that how different PCBs associate with phospholipid bilayers must be reasoned from the available experimental evidence since direct structural determination does not yet exist. Jonker and van der Heijden do not disagree with our experiments but claim to find inconsistency in the discussion and tentative model that we had proposed.