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Reduction of mitomycin C is catalysed by human recombinant NRH:quinone oxidoreductase 2 using reduced nicotinamide adenine dinucleotide as an electron donating co-factor

Lookup NU author(s): Dr David Jamieson, Professor Alan Boddy


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NRH:Quinone Oxidoreductase 2 (NQO2) has been described as having no enzymatic activity with nicotinamide adenine dinucleotide (NADH) or NADPH as electron donating cosubstrates. Mitomycin C (MMC) is both a substrate for and a mechanistic inhibitor of the NQO2 homologue NQO1. NRH:quinone oxidoreductase 2 catalysed the reduction of MMC at pH 5.8 with NADH as a co-factor. This reaction results in species that inhibit the NQO2-mediated metabolism of CB1954. In addition, MMC caused an increase in DNA cross-links in a cell line transfected to overexpress NQO2 to an extent comparable to that observed with an isogenic NQO1-expressing cell line. These data indicate that NQO2 may contribute to the metabolism of MMC to cytotoxic species. © 2006 Cancer Research UK.

Publication metadata

Author(s): Jamieson, D., Tung, A., Knox, R., Boddy, A.

Publication type: Article

Publication status: Published

Journal: British Journal of Cancer

Year: 2006

Volume: 95

Issue: 9

Pages: 1229-1233

Print publication date: 06/11/2006

ISSN (print): 0007-0920

ISSN (electronic): 1532-1827


DOI: 10.1038/sj.bjc.6603414

PubMed id: 17031400


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