Redox Enzyme Wiring to Surfaces
The interface between the organic (or biological) to the inorganic is one of the major focuses of our lab. Enzymes or proteins that are efficiently coupled with electrodes made of metals or graphene, are the basis for many types of devices that enable electron communication with electrodes. One of the most basic hypotheses in the lab was that by orienting redox enzymes on electrodes to afford a minimal distance for electron transfer to the redox active-site in the protein, electron injection or electron withdrawal will become very efficient and will allow a potentiometric control of the enzyme activity. When the attachment is done through a single point, the interference with the protein/enzyme folding becomes minimal. Such devices can be enzyme-based biosensors, enzyme-based fuel-cells, autonomous biosensing devices and wearable biosensing devices.
Enzymes that we have site-specifically wired to electrodes are: Copper efflux oxidase from E. coli (CueO) and a fusion enzyme of glucose dehydrogenase with a minimal cytochrome domain (FGM).
Genetic Code Expansion in Different Microorganisms
In order to modify proteins and enzymes in different organisms, we have expanded the genetic code of the following microorganisms:
By expanding the genetic code of Pseudomonas aeruginosa we could now click to an unnatural amino acid a fluorophore and track flagella in a living biofilm: