Hydrogen and methane fuel production relies on enzymes that are as fast and efficient as platinum, but scientists have been unable to see how electrons move through them during catalysis. Existing bio-electrochemistry methods, developed in the 1980s, can probe an enzyme’s active site but cannot map the electron-transfer processes that drive the reaction. This project will build a new technique that combines advanced computation with light-activated chemistry to attach enzymes to electrodes in a controlled way, allowing researchers to separate and model each electron-transfer step. The team will test the method on two enzyme families: LPMOs, which break down cellulose in biorefinery cocktails, and hydrogenases, which split or produce hydrogen as efficiently as platinum. If successful, the toolkit could accelerate the design of biofuel catalysts that use abundant metals like iron and nickel instead of rare, expensive platinum. This is fundamental science—it will not produce a working fuel cell tomorrow—but understanding how nature moves electrons so efficiently could eventually reshape how we produce clean hydrogen and methane from water and carbon dioxide.
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In Nature the production of hydrogen and methane fuel molecules from readily available starting materials such as water and carbon dioxide is achieved selectively, efficiently and rapidly by electrocatalytic redox-metalloenzymes containing non-precious transition metal active sites. The outstanding recent scientific advances made in molecular biology have made the development of biofuel technologies based on these enzymes a reality, but such applications require a complementary toolkit of physical chemistry methods that can dissect how DNA sequence and protein structure relates to function. Classic bio-electrochemistry methods developed in the 1980s have been a powerful way to probe the active site reactivity of such enzymes, but they have been unable to map the electron transfer processes which underpin the catalysis. Therefore, we have been limited to a narrowly active-site focussed view of enzyme mechanism. This project will transform the state of the art in bio-electrochemistry to deliver a powerful new technique that can "see" the electron-transfer processes of the highly evolved and essential electron-transfer reaction centres in redox-enzymes, and deconvolute their role in electrocatalysis. This will be achieved by deploying advanced computational methods to integrate intelligent experimental design into electrochemistry to develop a methodology that lets us separate and accurately model the electron transfer processes of an enzyme bound to substrate, and chemical biology methods to develop linker molecules for light-activated electrografting of proteins and enzymes onto electrodes. We will showcase the power of this new electrochemical enzymology toolkit by conducting previously impossible hypothesis-led investigations and enzyme-discovery projects into i) cellulose-degrading LPMOs that play a crucial role in biorefinery enzyme cocktails and ii) hydrogenases, Ni+Fe or Fe-only metalloenzymes that are as rapid and efficient at hydrogen-catalysis as platinum.
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