Breaking the barrier to fast electron transfer

A study of the electron transfer for a non-glycosylated redox variant of GOx is reported, immobilised onto an electrode via a polyhistidine tag. The non-glycosylated variant allows the enzyme to be brought closer to the electrode, and within charge transfer distances predicted by Marcus' theory. The enzyme-electrode-hybrid shows direct very fast reversible electrochemical electron transfer, with a rate constant of ~ 350 s^− 1 under anaerobic conditions. This is 2 orders of magnitude faster than the enzyme-free flavin adenine dinucleotide (FAD). These results are discussed in the context of the conformation of FAD in the active site of GOx. Further data, presented in the presence of oxygen, show a reduced electron transfer rate (~ 160 s^− 1) that may be associated with the oxygen interaction with the histidines in the active site. These residues are implicated in the proton transfer mechanism and thus suggest that the presence of oxygen may have a profound effect in attenuating the direct electron transfer rate and thus moderating ‘short-circuit’ incidental electron transfer between proteins.