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Possible direct involvement of the active‐site [4Fe–4S] cluster of the GcpE enzyme from Thermus thermophilus in the conversion of MEcPP
Author(s) -
Adedeji Dolapo,
Hernandez Heather,
Wiesner Jochen,
Köhler Uwe,
Jomaa Hassan,
Duin Evert C.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.026
Subject(s) - thermus thermophilus , active site , chemistry , cluster (spacecraft) , thermus , enzyme , biochemistry , stereochemistry , thermophile , computer science , escherichia coli , gene , programming language
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.