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Страница 1 от 32 полученные результаты
Solubilization of the alternative oxidase of cuckoo-pint (Arum maculatum) mitochondria. Stimulation by high concentrations of ions and effects of specific inhibitors.
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Selective solubilization of cyanide- and antimycin-insensitive duroquinol oxidase activity from cuckoo-pint (Arum maculatum) mitochondria was achieved using taurocholate. Inhibitor-sensitivities and water-forming DQH2 (tetramethyl-p-hydroquinone, reduced form): O2 stoichiometry were the same for the
Identification of a gene for pyruvate-insensitive mitochondrial alternative oxidase expressed in the thermogenic appendices in Arum maculatum.
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Heat production in thermogenic plants has been attributed to a large increase in the expression of the alternative oxidase (AOX). AOX acts as an alternative terminal oxidase in the mitochondrial respiratory chain, where it reduces molecular oxygen to water. In contrast to the mitochondrial terminal
Discrimination between duroquinol oxidase activity and the terminal oxidation step of the cyanide-resistant electron transport pathway of plant mitochondria.
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Comparison of the cyanide-resistant duroquinol oxidase activity of sub-mitochondrial particles from Arum maculatum L. with their ability to carry out a cyanide-resistant oxidation of NADH and succinate shows that heat-inactivation of the duroquinol oxidase activity does not proportionally affect
[Isolation of the alternative oxidase from Arum maculatum].
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There is plenty of alternate oxidase (AOX) in the inflorescences of thermogenic A rum maculatum. The isolated mitochondria exhibited a high activity, consuming oxygen on average 32 micromoles/min. The concentration of the isolated protein from mitochondria was 14.0 mg/ml. The isolated mitochondria
Regulation of thermogenesis in flowering Araceae: the role of the alternative oxidase.
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The inflorescences of several members of the Arum lily family warm up during flowering and are able to maintain their temperature at a constant level, relatively independent of the ambient temperature. The heat is generated via a mitochondrial respiratory pathway that is distinct from the cytochrome
Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants.
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The subcellular location of two enzymes in the biosynthetic pathway for protoporphyrin IX, coproporphyrinogen (coprogen) oxidase (EC 1.3.3.3) and protoporphyrinogen (protogen) oxidase (EC 1.3.3.4) has been investigated in etiolated pea (Pisum sativum) leaves and spadices of cuckoo-pint (Arum
Engineering plant alternative oxidase function in mammalian cells: substitution of the motif-like sequence ENV for QDT diminishes catalytic activity of Arum concinnatum AOX1a expressed in HeLa cells.
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Alternative oxidase (AOX) is a nonproton motive quinol-oxygen oxidoreductase which is a component of the mitochondrial respiratory chain in higher plants. In this study, we have characterized the catalytic activity and regulatory behaviors of Arum concinnatum AOX isoforms, namely AcoAOX1a and
A novel functional element in the N-terminal region of Arum concinnatum alternative oxidase is indispensable for catalytic activity of the enzyme in HeLa cells.
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Alternative oxidase (AOX) is a quinol-oxygen oxidoreductase, which is known to possess a dicarboxylate diiron reaction center held in structurally postulated alpha-helical bundle. However, little is known about the structural or functional features of its N-terminal region in any organism, with the
Activation of the plant alternative oxidase by high reduction levels of the Q-pool and pyruvate.
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This report describes the activation of the alternative oxidase (AOX) of higher plant mitochondria by a high reduction level of the ubiquinone pool in the presence of pyruvate. In mitochondria from both thermogenic (Arum italicum spadices) and nonthermogenic (Glycine max cotyledons) tissues AOXis
Purification of the plant alternative oxidase from Arum maculatum: measurement, stability and metal requirement.
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We have purified plant alternative oxidase (AOX) protein from the spadices of thermogenic Arum maculatum (cuckoo pint) to virtual homogeneity. The obtained enzyme fraction exhibits a high specific activity, consuming on average 32 micromol oxygen min(-1) mg(-1), which is completely stable for at
Interaction of purified alternative oxidase from thermogenic Arum maculatum with pyruvate.
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Plant alternative oxidase (AOX) activity in isolated mitochondria is regulated by carboxylic acids, but reaction and regulatory mechanisms remain unclear. We show that activity of AOX protein purified from thermogenic Arum maculatum spadices is sensitive to pyruvate and glyoxylate but not succinate.
Partial Purification and Characterization of the Quinol Oxidase Activity of Arum maculatum Mitochondria.
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The menadiol oxidase activity of Arum maculatum mitochondria has been solubilized and fractionated. A preparation has been obtained which has an increased specific activity and a greatly decreased polypeptide composition when compared to the mitochondria. This preparation retains normal inhibitor
New inhibitors of the ubiquinol oxidase of higher plant mitochondria.
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A screen has been performed of possible inhibitors of the ubiquinol oxidase of higher plant mitochondria by assaying their effects on cyanide-insensitive NADH oxidase of mitochondria of Arum maculatum. A number of compounds which have powerful inhibitory effects have been identified. Potent
Degradation of mitochondrial alternative oxidase in the appendices of Arum maculatum
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Cyanide-resistant alternative oxidase (AOX) is a nuclear-encoded quinol oxidase located in the inner mitochondrial membrane. Although the quality control of AOX proteins is expected to have a role in elevated respiration in mitochondria, it remains unclear whether thermogenic plants possess
Substrate Kinetics of the Plant Mitochondrial Alternative Oxidase and the Effects of Pyruvate.
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The kinetics of alternative oxidase (AOX) of Arum italicum spadices and soybean (Glycine max L.) cotyledons were studied both with intact mitochondria and with a solubilized, partially purified enzyme. Ubiquinone analogs were screened for their suitability as substrates and ubiquinol-1 was found to
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