| Literature DB >> 20534343 |
Fabien Pierrel1, Olivier Hamelin, Thierry Douki, Sylvie Kieffer-Jaquinod, Ulrich Mühlenhoff, Mohammad Ozeir, Roland Lill, Marc Fontecave.
Abstract
Yeast ubiquinone or coenzyme Q(6) (Q(6)) is a redox active lipid that plays a crucial role in the mitochondrial electron transport chain. At least nine proteins (Coq1p-9p) participate in Q(6) biosynthesis from 4-hydroxybenzoate (4-HB). We now show that the mitochondrial ferredoxin Yah1p and the ferredoxin reductase Arh1p are required for Q(6) biosynthesis, probably for the first hydroxylation of the pathway. Conditional Gal-YAH1 and Gal-ARH1 mutants accumulate 3-hexaprenyl-4-hydroxyphenol and 3-hexaprenyl-4-aminophenol. Para-aminobenzoic acid (pABA) is shown to be the precursor of 3-hexaprenyl-4-aminophenol and to compete with 4-HB for the prenylation reaction catalyzed by Coq2p. Yeast cells convert U-((13)C)-pABA into (13)C ring-labeled Q(6), a result that identifies pABA as a new precursor of Q(6) and implies an additional NH(2)-to-OH conversion in Q(6) biosynthesis. Our study identifies pABA, Yah1p, and Arh1p as three actors in Q(6) biosynthesis. 2010 Elsevier Ltd. All rights reserved.Entities:
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Year: 2010 PMID： 20534343 DOI： 10.1016/j.chembiol.2010.03.014
Source DB: PubMed Journal: Chem Biol ISSN： 1074-5521