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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Seemann M,Tse Sum Bui B,Wolff M,Miginiac-Maslow M,Rohmer Mdoi
10.1016/j.febslet.2006.01.082keywords:
subject
Has Abstractpub_date
2006-03-06 00:00:00pages
1547-52issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00152-9journal_volume
580pub_type
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