Wednesday, October 19, 2011

Biosynthesis of Isoprene Units: Mössbauer Spectroscopy of Substrate and Inhibitor Binding to the [4Fe-4S] Cluster of the LytB/IspH Enzyme

Biosynthesis of Isoprene Units: Mössbauer Spectroscopy of Substrate and Inhibitor Binding to the [4Fe-4S] Cluster of the LytB/IspH Enzyme: Thumbnail image of graphical abstract

A fascinating cube: LytB, an enzyme containing a [4Fe-4S] cluster, catalyzes the last step of the methylerythritol phosphate pathway, a target for antibacterial and antiparasitic drugs. Field-dependent Mössbauer spectroscopy showed that the unique fourth iron atom of the [4Fe-4S] cluster coordinates to the hydroxy group of the substrate (see picture) and to the amino and thiol moieties of two potent inhibitor substrate analogues.

No comments:

Post a Comment