Working towards a more sustainable society inevitably goes through developing a healthy manufacturing industry that fulfils our societal needs in an economically sustainable and environmentally friendly manner. Among all issues that need to be overcome to get to that aim, a more sustainable industrial chemical synthesis for manufacturing of added value materials, such us drugs, high-specs polymers, etc., needs to be developed. Currently, employed catalytic methods herein often require economically unbearable use of highly expensive catalysts, energetically unfavourable reaction conditions, and use of highly contaminant non-aqueous chemical components. As in many other disciplines, nature teaches us lessons on how to do that in a much more efficient, sustainable way via enzymatic catalysis. Enzymes are able to catalyse key reactions for us at superior rates of several orders of magnitude compared to synthetic paths, and under very mild (ambient) conditions using a fully green aqueous chemistry. Enzymatic catalysis is one of those disciplines in molecular biology where the crystal structure has been unable to bring a definitive mechanistic picture on such an outstanding catalytic process. Knowing the “secrets” of enzymatic catalysis is a major call and a priority in providing sustainability for the future generations. While a number of hypotheses based on pure chemical interactions have attempted to explain enzymatic catalysis in a number of enzyme proteins, this has not yet provided a universal picture on how the reactions are being significantly sped up in an enzyme active site. The Biophysics field has abundantly shown how forces can play key roles in essential biological functions, e.g. the emerging field of mechanobiology shows us how mechanical forces are regulated at the molecular level to control cell functions. A plausible, yet experimentally untested, hypothesis states that nature has also mastered the exploitation of force fields to control chemical reactivity. Fields4CAT focuses on this issue by proposing a unique set of experiments combining single-protein trapping in a nanogap (with full control over applied high force fields) with site-specific protein mutagenesis. This unique approach allows orientation-controlled trapping of individual enzymes in a nanoscale tunelling gap while continuously monitoring the tunelling current flowing through the protein structure. Abrupt changes in the transient tunnelling current are indicative of enzyme activity (see Summary Figure below) and allow for electrical characterization of enzymatic activity in a single enzyme. The enzymatic activity can be then studied under the application of external force fields stimuli along the nanoscale junction. Revealing the details of how force fields affect enzymatic processes will undoubtedly open to “new ways” of doing more sustainable chemical synthesis by either artificially boosting the enzyme’s enzymatic capabilities or by mimicking the main chemical principles of enzymatic catalysis.
