Welcome to another insightful episode, where today we have the pleasure of hosting Dr. Grinter, a leading authority on bacterial metabolism. Dr. Grinter will illuminate his latest research unraveling the process and mechanisms of atmospheric H2 oxidation in aerobic bacteria, a process with significant global implications, from regulating the composition of the atmosphere to driving primary production in extreme environments.

Dr. Grinter provides an in-depth explanation of his research on the Mycobacterium smegmatis hydrogenase Huc, a highly efficient oxygen-insensitive enzyme. His research team's success in determining the cryo-electron microscopy structure of this enzyme offers key insights into its function.

One of the most fascinating discoveries is the enzyme's unique capability to use narrow hydrophobic gas channels to selectively bind atmospheric H2 over O2 and the role of 3 [3Fe–4S] clusters in making atmospheric H2 oxidation energetically feasible. Further, he elaborates on how Huc couples the oxidation of atmospheric H2 to the hydrogenation of the respiratory electron carrier menaquinone.

Dr. Grinter delves into the intriguing octameric structure of the Huc catalytic subunits and its role in transporting and reducing menaquinone far from the membrane. His research uncovers a unique mode of energy coupling dependent on long-range quinone transport.

Join us in this enlightening episode to better understand the biogeochemically and ecologically critical process of atmospheric H2 oxidation. Dr. Grinter's research paves the way for the development of catalysts that oxidize H2 in ambient air, offering far-reaching implications for our understanding of bacterial metabolism and the broader field of biochemistry.

Grinter, R., Kropp, A., Venugopal, H. et al. Structural basis for bacterial energy extraction from atmospheric hydrogen. Nature 615, 541–547 (2023). https://doi.org/10.1038/s41586-023-05781-7