|Related Categories||Biochemicals and Reagents, Cell Biology, Cofactor, Cofactors, Cofactors and Substrates,|
Analog of coenzyme Q10 (not naturally occurring)
Tandem Mass Spectrometry data independently generated by Scripps Center for Metabolomics is available to view or download in PDF. C7956.pdf Tested metabolites are featured on Scripps Center for Metabolomics METLIN Metabolite Database. To learn more, visit sigma.com/metlin.
Coenzyme Q1 (CoQ1) is a 1 isoprenyl group (not naturally occurring) member of a family of ubiquinones that share a quinine chemical group but differ in the number of isoprenyl chemical subunits in their tail. The CoQ compounds are lipid soluble components of cell membranes where they perform multiple functions such as electron and proton transport. The most well studied CoQ compound is CoQ10. CoQ1 is frequently used in comparison studies on the effect of isoprenyl chain length on CoQ functions or distribution and to identify quinone reductases.
Genetic evidence for NAD(P)H:quinone oxidoreductase 1-catalyzed quinone reduction on passage through the mouse pulmonary circulation. Lindemer BJ, Bongard RD, et al. Am. J. Physiol. Lung Cell. Mol. Physiol. 300, L773-780, (2011)
Coenzyme Q(1) as a probe for mitochondrial complex I activity in the intact perfused hyperoxia-exposed wild-type and Nqo1-null mouse lung. Bongard RD, Myers CR, Lindemer BJ, et al. Am. J. Physiol. Lung Cell. Mol. Physiol. 302(9), L949-58, (2012)
Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (Complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes. Ohnishi T, Ohnishi ST, Shinzawa-Ito K, et al. Biofactors 32(1-4), 13-22, (2008)
Role of mitochondrial electron transport complex I in coenzyme Q1 reduction by intact pulmonary arterial endothelial cells and the effect of hyperoxia. Merker MP, Audi SH, Lindemer BJ, et al. Am. J. Physiol. Lung Cell. Mol. Physiol. 293(3), L809-19, (2007)
Inhibitory effect of coenzyme Q on eukaryotic DNA polymerase gamma and DNA topoisomerase II activities on the growth of a human cancer cell line. Yonezawa Y, Kuriyama I, Fukuoh A, et al. Cancer Sci. 97(8), 716-23, (2006)
Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Calabrese V, Scapagnini G, Ravagna A, et al. Neurochem. Res. 28(9), 1321-8, (2003)
Decreases in serum ubiquinone concentrations do not result in reduced levels in muscle tissue during short-term simvastatin treatment in humans. Laaksonen R, Jokelainen K, Sahi T, et al. Clin. Pharmacol. Ther. 57(1), 62-6, (1995)
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