Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: direct thylakoid/ferredoxin-dependent photoreduction of GcpE/IspG |
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Authors: | Seemann Myriam Tse Sum Bui Bernadette Wolff Murielle Miginiac-Maslow Myroslawa Rohmer Michel |
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Institution: | Université Louis Pasteur/CNRS, Institut de Chimie LC3/UMR 7177, 4 rue Blaise Pascal, 67070 Strasbourg Cedex, France. |
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Abstract: | In the methylerythritol phosphate pathway for isoprenoid biosynthesis, the GcpE/IspG enzyme catalyzes the conversion of 2-C-methyl-d-erythritol 2,4-cyclodiphosphate into (E)-4-hydroxy-3-methylbut-2-enyl diphosphate. This reaction requires a double one-electron transfer involving a 4Fe-4S] cluster. A thylakoid preparation from spinach chloroplasts was capable in the presence of light to act as sole electron donor for the plant GcpE Arabidopsis thaliana in the absence of any pyridine nucleotide. This is in sharp contrast with the bacterial Escherichia coli GcpE, which requires flavodoxin/flavodoxin reductase and NADPH as reducing system and represents the first proof that the electron flow from photosynthesis can directly act in phototrophic organisms as reducer in the 2-C-methyl-d-erythritol 4-phosphate pathway, most probably via ferredoxin, in the absence of any reducing cofactor. In the dark, the plant GcpE catalysis requires in addition of ferredoxin NADP(+)/ferredoxin oxido-reductase and NADPH as electron shuttle. |
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Keywords: | DMAPP dimethylallyl diphosphate GcpE IspG HMBPP synthase HMBPP (E)-4-hydroxy-3-methylbut-2-enyl diphosphate IPP isopentenyl diphosphate LytB IspH HMBPP reductase MEcDP d-erythritol 2" target="_blank">2-C-methyl-d-erythritol 2 4-cyclodiphosphate MEP d-erythritol 4-phosphate" target="_blank">2-C-methyl-d-erythritol 4-phosphate |
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