Possible direct involvement of the active-site [4Fe-4S] cluster of the GcpE enzyme from Thermus thermophilus in the conversion of MEcPP

被引：23
作者：
Adedeji, Dolapo
Hernandez, Heather
Wiesner, Jochen
Koehler, Uwe
Jomaa, Hassan
Duin, Evert C.
机构：
[1] Auburn Univ, Dept Chem & Biochem, Auburn, AL 36849 USA
[2] Univ Georgia, Dept Chem, Athens, GA 30602 USA
[3] Univ Georgia, Ctr Metalloenzyme Studies, Athens, GA 30602 USA
[4] Univ Giessen Klinikum, Inst Klin Chem & Pathobiochem, D-35392 Giessen, Germany
[5] Eurofins Medigenom GmbH, D-82152 Martinsried, Germany
来源：
FEBS LETTERS | 2007年 / 581卷 / 02期
关键词：
GcpE; 2-C-methyl-D-erythritol-2,4-cyclodiphosphate; 4Fe-4S; EPR spectroscopy; resonance Raman spectroscopy; isoprene synthesis;
D O I：
10.1016/j.febslet.2006.12.026
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The GcpE enzyme converts 2-C-methyl-D-erythritol-2,4-cyclodiphosphate (MEcPP) into (E)-4-hydroxy-3-methylbut-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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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收藏
页码：279 / 283
页数：5
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