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Rugolo M, Zannoni D. Oxidation of External NAD(P)H by Jerusalem Artichoke (Helianthus tuberosus) Mitochondria : A Kinetic and Inhibitor Study. Plant Physiol. 1992;99(3):1037-43doi: 10.1104/pp.99.3.1037.
Rugolo, M., & Zannoni, D. (1992). Oxidation of External NAD(P)H by Jerusalem Artichoke (Helianthus tuberosus) Mitochondria : A Kinetic and Inhibitor Study. Plant physiology, 99(3), 1037-43. https://doi.org/10.1104/pp.99.3.1037
Rugolo, M, and Zannoni, D. "Oxidation of External NAD(P)H by Jerusalem Artichoke (Helianthus tuberosus) Mitochondria : A Kinetic and Inhibitor Study." Plant physiology vol. 99,3 (1992): 1037-43. doi: https://doi.org/10.1104/pp.99.3.1037
Rugolo M, Zannoni D. Oxidation of External NAD(P)H by Jerusalem Artichoke (Helianthus tuberosus) Mitochondria : A Kinetic and Inhibitor Study. Plant Physiol. 1992 Jul;99(3):1037-43. doi: 10.1104/pp.99.3.1037. PMID: 16668968; PMCID: PMC1080581.
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Plant Physiol. 1992 Jul;99(3):1037-43. doi: 10.1104/pp.99.3.1037.

Oxidation of External NAD(P)H by Jerusalem Artichoke (Helianthus tuberosus) Mitochondria : A Kinetic and Inhibitor Study.

Plant physiology

M Rugolo, D Zannoni

Affiliations

  1. Department of Biology, Biochemistry Laboratory, University of Bologna, 40126 Bologna Italy.

PMID: 16668968 PMCID: PMC1080581 DOI: 10.1104/pp.99.3.1037

Abstract

The functional interaction between the externally located NAD(P)H dehydrogenase and the Q-pool acceptor site(s) in Percoll-purified mitochondria from Jerusalem artichoke (Helianthus tuberosus L. cv OB1) mitochondria has been investigated. Oxidation of exogenous NADH is stimulated by ubiquinone (UQ(1)) with a parallel decrease of the apparent K(m) for NADH. In the presence of saturating amounts of UQ(1) as electron acceptor, the K(m) (NADH) is not affected by variations of the ionic strength. Conversely, the K(m) for UQ(1) is decreased by the screening effect of negative charges on the outer membrane surface. Under low-ionic strength, the hydroxyflavone platanetin progressively inhibits NADH oxidation with a mean inhibition dose of approximately 3 nanomoles of inhibitor per milligram of protein. Interestingly, under high-ionic strength, oxidation of NADH proceeds through two platanetin binding sites, one of which has a lower affinity for the inhibitor (mean inhibition dose = 20 nanomoles per milligram protein), because it is located near the outer surface of the membrane. This latter site is the one involved in the oxidation of external NADPH and, possibly, also affected by spermine and spermidine. Similarly to NADH, oxidation of NADPH is fully sensitive to micromolar concentrations of free Ca(2+) ions; in addition, similar concentrations of the sulfhydryl reagent mersalyl are required to inhibit both NADH and NADPH oxidative activities. The results are interpreted as evidence for the presence of a single nonspecific NAD(P)H dehydrogenase.

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