| Literature DB >> 17214985 |
Dolapo Adedeji1, Heather Hernandez, Jochen Wiesner, Uwe Köhler, Hassan Jomaa, Evert C Duin.
Abstract
The GcpE enzyme converts 2-C-methyl-D-erythritol-2,4-cyclodiphosphate (MEcPP) into (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate (HMBPP) in the penultimate step of the DOXP pathway for isoprene biosynthesis. Purification of the enzyme under exclusion of air leads to a preparation that contains solely [4Fe-4S] clusters. Kinetic studies showed that in the presence of the artificial reductant dithionite and MEcPP a new transient iron-sulfur-based signal is detected in electron paramagnetic resonance (EPR) spectroscopy. Similarity of this EPR signal to that detected in ferredoxin:thioredoxin reductase indicates that during the reaction an intermediate is directly bound to the active-site cluster.Entities:
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Year: 2006 PMID： 17214985 DOI： 10.1016/j.febslet.2006.12.026
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124