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. 1995 May 23;92(11):4887–4891. doi: 10.1073/pnas.92.11.4887

Coenzyme Q reductase from liver plasma membrane: purification and role in trans-plasma-membrane electron transport.

J M Villalba 1, F Navarro 1, F Córdoba 1, A Serrano 1, A Arroyo 1, F L Crane 1, P Navas 1
PMCID: PMC41812  PMID: 7761418

Abstract

A specific requirement for coenzyme Q in the maintenance of trans-plasma-membrane redox activity is demonstrated. Extraction of coenzyme Q from membranes resulted in inhibition of NADH-ascorbate free radical reductase (trans electron transport), and addition of coenzyme Q10 restored the activity. NADH-cytochrome c oxidoreductase (cis electron transport) did not respond to the coenzyme Q status. Quinone analogs inhibited trans-plasma-membrane redox activity, and the inhibition was reversed by coenzyme Q. A 34-kDa coenzyme Q reductase (p34) has been purified from pig-liver plasma membranes. The isolated enzyme was sensitive to quinone-site inhibitors. p34 catalyzed the NADH-dependent reduction of coenzyme Q10 after reconstitution in phospholipid liposomes. When plasma membranes were supplemented with extra p34, NADH-ascorbate free radical reductase was activated but NADH-cytochrome c oxidoreductase was not. These results support the involvement of p34 as a source of electrons for the trans-plasma-membrane redox system oxidizing NADH and support coenzyme Q as an intermediate electron carrier between NADH and the external acceptor ascorbate free radical.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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