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Papers In Press, published online ahead of print July 2, 2001
J. Biol. Chem, 10.1074/jbc.C100346200
Submitted on June 21, 2001
Revised on July 2, 2001
Accepted on July 1, 2001
Biochemistry and Biophysics, Stockholm University, Stockholm S-106 91
Corresponding Author: berthold{at}dbb.su.se
Ubiquinone (UQ) is an essential cofactor for respiratory metabolism. In yeast, mutation of the COQ7 gene results in the absence of UQ biosynthesis and demonstrates a role for this gene in the step leading to the hydroxylation of 5-demethoxyubiquinone (DMQ). Intriguingly, the disruption of the corresponding gene in Caenorhabditis elegans, clk-1, results in a prolonged lifespan and a slowing of development. Due to the pleiotropic effect of this disruption, the small size of the protein, and the lack of obvious homology to other known hydroxylases, it has been suggested that Coq7 may be a regulatory or structural component in UQ biosynthesis, rather than acting as the hydroxylase per se. Here we identify Coq7 as belonging to a family of a di-iron containing oxidases/hydroxylases based on a conserved sequence motif for the iron ligands, supporting a direct function of Coq7 as a hydroxylase. We have cloned COQ7 from Pseudomonas aeruginosa and Thiobacillus ferrooxidans and show that indeed this gene complements an E. coli mutant which lacks an unrelated DMQ hydroxylase. Based on the similarities to other well-studied di-iron carboxylate proteins, we propose a structural model for Coq7 as an interfacial integral membrane protein, and discuss substrate binding and catalysis.
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