Resonance Raman Spectroscopic Study of the Unusual [4Fe-4S]²⁺ Cluster of IspH, the Last Enzyme of the Methylerythritol Phosphate Pathway for Terpenoid Biosynthesis.

ABSTRACT: IspH is the last enzyme of the methylerythritol phosphate pathway. It catalyzes the reductive dehydroxylation of (E)-4-hydroxy-3-methyl-but-2-en-1-yl diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), which are precursors for the biosynthesis of terpenoids, essential molecules for the survival of all living organisms. This pathway is absent in humans, making it a promising target for drug discovery. Escherichia coli IspH harbors an unusual [4Fe-4S]²⁺ cluster linked to three conserved cysteines with a unique iron site proposed to be coordinated to three water molecules. Here, the first resonance Raman spectroscopic study of the cluster of IspH in the 2+ oxidation state is reported. Using isotopic labeling with ²H₂O and H

SUBMITTER: Jobelius H 

PROVIDER: S-EPMC12447371 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature