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Publication Abstract from PubMed

Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known.

ubiI, a New Gene in Escherichia coli Coenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation.,Hajj Chehade M, Loiseau L, Lombard M, Pecqueur L, Ismail A, Smadja M, Golinelli-Pimpaneau B, Mellot-Draznieks C, Hamelin O, Aussel L, Kieffer-Jaquinod S, Labessan N, Barras F, Fontecave M, Pierrel F J Biol Chem. 2013 Jul 5;288(27):20085-92. doi: 10.1074/jbc.M113.480368. Epub 2013, May 24. PMID:23709220^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.