Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy

Abstract

Sulfur's balancing act in cytochrome c Cytochrome c enzymes have two distinct functions that depend on the position of a methionine residue. When the sulfur in the methionine side chain coordinates with iron in the enzyme's active site, the protein is optimized for electron transfer; otherwise, it is poised for peroxidase activity. Mara et al. used ultrafast x-ray absorption and emission spectroscopy to probe the energetics of this Fe-S bond (see the Perspective by Bren and Raven). By breaking the bond transiently with light and then timing its reformation, they determined that the surrounding protein environment boosts the bond strength by 4 kilocalories per mole—just enough to toggle between each functional state at a practical rate. Science , this issue p. 1276 ; see also p. 1236