During enzyme catalysis, the initial substrate can undergo a number of changes at the active site and transform into a product, analogous to atomic level origami. The elucidation of the so called intermediates are critical in understanding enzymatic function and can help us design bio-inspired catalysts or new inhibitors against pathogens. I aim to chemically define and capture intermediates of membrane bound enzymes (i.e., ATPases, oxidoreductases) 'at work' using biochemical, spectroscopic and advanced structural biology. Capturing and visualising proteins during intermediate states will allow ‘molecular movies’ of biological complexes to be made, bringing unprecedented insight into protein function at a chemical level to enhance the fields of novel pharmaceutical, therapeutic and catalyst development.