Bonnie Murphy obtained her doctorate in the field of inorganic biochemistry and spectroscopy of complex metalloenzymes that require metal-containing cofactors for the reactions they catalyse. During her time as a postdoctoral researcher, she used cryo-electron microscopy to describe the first structure of the intact mitochondrial enzyme “ATP synthase” at molecular resolution. This is a transmembrane protein that plays an important role in the cellular energy balance and therefore in almost all processes in the organism. With her working group, Murphy was also able to identify other important structures: that of a large enzyme complex that converts CO2 into methane, and the structure of an enzyme that produces hydrogen. Both works are not least significant from the point of view of society since they provide insights for the biotechnological production of chemical energy storage systems and for tackling climate change.