FEBS Lett. 1992 Dec 21;314(3):331-4.

A novel ubiquinone reductase activity in rat cytosol.

Takahashi T, Shitashige M, Okamoto T, Kishi T, Goshima K.

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Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.

Abstract

Ubiquinone (UQ) reductase activity which reduces UQ to ubiquinol (UQH2) in rat tissues was roughly proportional to the UQH2/total UQ ratio in respective tissues. The highest activity was found in the liver, showing the highest UQH2/total UQ ratio. A greater part of liver UQ reductase activity was located in the cytosol. Within a week, the liver UQ reductase activity decreased by 80% even at -20 degrees C. The DT-diaphorase activity was stable. UQ reductase required NADPH as the hydrogen donor and was not inhibited by a less than 1 microM concentration of dicoumarol. There was no stimulation of UQ reductase in the presence of bovine serum albumin nor in Triton X-100. Yet, both stimulated DT-diaphorase. As a result, UQ reductase appeared to be a novel NADPH-UQ oxidoreductase and responsible for the UQ redox state in liver.

PMID:: 1468565; [PubMed - indexed for MEDLINE]

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