Venue: Biomedicum, D0320

Speaker: Nobel Laureate in Chemistry 1997, Sir John E. Walker, MRC Mitochondrial Biology Unit, Cambridge, UK

Walker’s landmark studies on the F1-ATPase from bovine heart mitochondria revealed the three catalytic sites in three different conformations that provided the binding change mechanism and rotary catalysis for the ATP synthase. This led to Walker’s share of the 1997 Nobel prize for chemistry. Since then, Walker and colleagues have produced most of the crystal structures in the PDB of mitochondrial ATP synthase, including transition state structures and protein with bound inhibitors and antibiotics. More recently, he has been using cryo-EM to visualise ATP synthases in action.

Walker was elected a Fellow of the Royal Society in 1995 and knighted in 1999. In 2012 he was awarded the Copley Medal.

Host: Nils-Goran Larsson, Nils-Goran.Larsson@ki.se