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Trost P, Foscarini S, Preger V, et al. Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane. Plant Physiol. 1997;114(2):737-746doi: 10.1104/pp.114.2.737.
Trost, P., Foscarini, S., Preger, V., Bonora, P., Vitale, L., & Pupillo, P. (1997). Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane. Plant physiology, 114(2), 737-746. https://doi.org/10.1104/pp.114.2.737
Trost, P., et al. "Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane." Plant physiology vol. 114,2 (1997): 737-746. doi: https://doi.org/10.1104/pp.114.2.737
Trost P, Foscarini S, Preger V, Bonora P, Vitale L, Pupillo P. Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane. Plant Physiol. 1997 Jun;114(2):737-746. doi: 10.1104/pp.114.2.737. PMID: 12223742; PMCID: PMC158359.
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Plant Physiol. 1997 Jun;114(2):737-746. doi: 10.1104/pp.114.2.737.

Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane.

Plant physiology

P. Trost, S. Foscarini, V. Preger, P. Bonora, L. Vitale, P. Pupillo

Affiliations

  1. Dipartimento di Biologia, Universita di Bologna, Bologna, Italy.

PMID: 12223742 PMCID: PMC158359 DOI: 10.1104/pp.114.2.737

Abstract

Quinone oxidoreductase activities dependent on pyridine nucleotides are associated with the plasma membrane (PM) in zucchini (Cucurbita pepo L.) hypocotyls. In the presence of NADPH, lipophilic ubiquinone homologs with up to three isoprenoid units were reduced by intact PM vesicles with a Km of 2 to 7 [mu]M. Affinities for both NADPH and NADH were similar (Km of 62 and 51 [mu]M, respectively). Two NAD(P)H:quinone oxidoreductase forms were identified. The first, labeled as peak I in gel-filtration experiments, behaves as an intrinsic membrane complex of about 300 kD, it slightly prefers NADH over NADPH, it is markedly sensitive to the inhibitor diphenylene iodonium, and it is active with lipophilic quinones. The second form (peak II) is an NADPH-preferring oxidoreductase of about 90 kD, weakly bound to the PM. Peak II is diphenylene iodonium-insensitive and resembles, in many properties, the soluble NAD(P)H:quinone oxidoreductase that is also present in the same tissue. Following purification of peak I, however, the latter gave rise to a quinone oxidoreductase of the soluble type (peak II), based on substrate and inhibitor specificities and chromatographic and electrophoretic evidence. It is proposed that a redox protein of the same class as the soluble NAD(P)H:quinone oxidoreductase (F. Sparla, G. Tedeschi, and P. Trost [1996] Plant Physiol. 112:249-258) is a component of the diphenylene iodonium-sensitive PM complex capable of reducing lipophilic quinones.

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