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PLANT PHYSIOLOGY , Vol 114, Issue 2 737-746, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Dissecting the Diphenylene Iodonium-Sensitive NAD(P)H:Quinone Oxidoreductase of Zucchini Plasma Membrane
P. Trost, S. Foscarini, V. Preger, P. Bonora, L. Vitale and P. Pupillo
Dipartimento di Biologia, Universita di Bologna, Bologna, Italy
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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