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.
CITATION STYLE
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
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