Ubiquinone-1 

Ubiquinone-1 is an intermediate in the synthesis of Coenzyme Q. Ubiquinone-1 can be reduced by NADPH oxidase, hepatoma cells, Ascorbic acid (HY-B0166)^{[1][2][3][4][5]}.

Ubiquinone-1 (60 µM) induces external deamino-NADH oxidation in potato tuber mitochondria by altering the specificity of an external Rotenone (HY-B1756)-insensitive NADH dehydrogenase^[1].
Ubiquinone-1 (100 µM) is rapidly and efficiently reduced to extracellularly detectable ubiquinol-1 by whole blood, isolated erythrocytes, and human hepatoma HepG2 cells^[3].
Ubiquinone-1 (150 µM) is reduced by NADPH oxidase of guinea pig macrophages under anaerobic conditions^[4].
Ubiquinone-1 is reduced by Ascorbic acid (HY-B0166) in a molecular oxygen concentration-controlled process^[5].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

250.29

C₁₄H₁₈O₄

727-81-1

Liquid

Orange to red

O=C1C(OC)=C(OC)C(C(C)=C1C/C=C(C)\C)=O

Room temperature in continental US; may vary elsewhere.

Solution, -20°C, 2 years

• [1]. Moller IM, et al. Ubiquinone-1 Induces External Deamino-NADH Oxidation in Potato Tuber Mitochondria. Plant Physiol. 1996 Sep;112(1):75-78.  [Content Brief]

  [2]. R Fato, et al. Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles. Biochemistry. 1996 Feb 27;35(8):2705-16.  [Content Brief]

  [3]. Stocker R, et al. Extracellular reduction of ubiquinone-1 and -10 by human Hep G2 and blood cells. Biochim Biophys Acta. 1993 Aug 20;1158(1):15-22.  [Content Brief]

  [4]. Murakami M, et al. NADPH oxidase of guinea-pig macrophages catalyses the reduction of ubiquinone-1 under anaerobic conditions. Biochem J. 1986 Jul 15;237(2):541-5.  [Content Brief]

  [5]. Roginsky VA, et al. Reduction of ubiquinone-1 by ascorbic acid is a catalytic and reversible process controlled by the concentration of molecular oxygen. Redox Rep. 1996 Feb;2(1):55-62.  [Content Brief]