Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (<i>E</i>)‐4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate reductase (LytB/IspH) from <i>Escherichia coli</i> is a [4Fe–4S] protein
Murielle Wolff(Centre National de la Recherche Scientifique), Myriam Seemann(Centre National de la Recherche Scientifique), Bernadette Tse Sum Bui(Centre National de la Recherche Scientifique), Yves‐Michel Frapart(Centre National de la Recherche Scientifique), Denis Tritsch(Centre National de la Recherche Scientifique), Ana Garcia Estrabot(Universitat de Barcelona), Manuel Rodrı́guez-Concepción(Universitat de Barcelona), Albert Boronat(Universitat de Barcelona), Andrée Marquet(Centre National de la Recherche Scientifique), Michel Rohmer(Centre National de la Recherche Scientifique)
Cited by 182Open Access
Abstract
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.
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