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Characterization of 1,4-benzoquinone reductase from bovine liver

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Abstract

1,4-Benzoquinone reductase was purified to electrophoretic homogeneity from bovine liver, and the purified enzyme found to have a molecular mass of 29 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited pH optimum between 8.0 and 8.5. The apparentK m for 1,4-benzoquinone was 1.643 mM, and the apparent Km for NADH was 1.837 mM. Various divalent cations, such as Hg2+, Cu2+, and Zn2+, exhibited strong inhibitory effects. The enzyme activity was also strongly inhibited by quercetin, dicumarol, and benzoic acid. Incubation of the enzyme withN-bromosuccinimide and pyridoxal 5′-phosphate led to inhibitions of 100% and 99%, respectively. Accordingly, these results suggest that tryptophan and lysine residues are involved at or near the active sites of the enzyme.

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  1. Department of Chemistry, Myong Ji University, 449-728, Yongin, Korea

    Kyungsoon Kim

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Kim, K. Characterization of 1,4-benzoquinone reductase from bovine liver. Biotechnol Bioproc E 7, 216–220 (2002). https://doi.org/10.1007/BF02932973

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