The last enzyme (LytB) of the methylerythritol phosphate pathway for isoprenoid biosynthesis catalyzes the reduction of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate into isopentenyl diphosphate and dimethylallyl diphosphate. This enzyme possesses a dioxygen-sensitive [4Fe-4S] cluster. This prosthetic group was characterized in the Escherichia coli enzyme by UV/visible and electron paramagnetic resonance spectroscopy after reconstitution of the purified protein. Enzymatic activity required the presence of a reducing system such as flavodoxin/flavodoxin reductase/reduced nicotinamide adenine dinucleotide phosphate or the photoreduced deazaflavin radical. © 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Wolff, M., Seemann, M., Tse Sum Bui, B., Frapart, Y., Tritsch, D., Garcia Estrabot, A., … Rohmer, M. (2003). Isoprenoid biosynthesis via the methylerythritol phosphate pathway: The (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein. FEBS Letters, 541(1–3), 115–120. https://doi.org/10.1016/S0014-5793(03)00317-X