Mitochondrial mechanism links protein folding to heme production and cell energy‎

Researchers at the University of Cologne have discovered a previously unknown mechanism that links two fundamental processes in mitochondria. The team, led by Julia Racho and Dylan Stobbe under the supervision of Professor Dr. Jan Riemer from the Institute of Biochemistry at the University of Cologne, demonstrated that the oxidative folding of proteins—that is, the process by which proteins acquire their functional three-dimensional structure and additional stabilizing disulfide bonds—is closely linked to the formation of heme. Heme is a vital component of the red blood pigment hemoglobin and is also required for energy production in cells, as well as for many other biological processes. The findings are published in the journal Science Advances.