Coenzyme Q. oxidized

Coenzyme Q (oxidized form) Coenzyme Q (reduced form)... 

The ready reversibility of this reaction is essential to the role that qumones play in cellular respiration the process by which an organism uses molecular oxygen to convert Its food to carbon dioxide water and energy Electrons are not transferred directly from the substrate molecule to oxygen but instead are transferred by way of an electron trans port chain involving a succession of oxidation-reduction reactions A key component of this electron transport chain is the substance known as ubiquinone or coenzyme Q... 

Two and twelve moles of ATP are produced, respectively, per mole of glucose consumed in the glycolytic pathway and each turn of the Krebs (citrate) cycle. In fat metaboHsm, many high energy bonds are produced per mole of fatty ester oxidized. Eor example, 129 high energy phosphate bonds are produced per mole of palmitate. Oxidative phosphorylation has a remarkable 75% efficiency. Three moles of ATP are utilized per transfer of two electrons, compared to the theoretical four. The process occurs via a series of reactions involving flavoproteins, quinones such as coenzyme Q, and cytochromes. 

The preparation of coenzyme Q usually iavolves either 2,3-dimethoxy-5-methylbenzoquinone or hydroquiaone as the starting material. Treatment of the hydroquiaone with geranyl bromide followed by oxidation affords (61, n = 2) (214). A facile and efficient preparation of ubiquiaone-10 (61, n = 10) has been developed (215). 

FIGURE 20.14 The succinate dehydrogenase reaction. Oxidation of succinate occurs with reduction of [FAD]. Reoxidation of [FADH9] transfers electrons to coenzyme Q. 

FIGURE 21.5 (a) The three oxidation states of coenzyme Q. (b) A space-filling model of coenzyme Q. 

In the third complex of the electron transport chain, reduced coenzyme Q (UQHg) passes its electrons to cytochrome c via a unique redox pathway known as the Q cycle. UQ cytochrome c reductase (UQ-cyt c reductase), as this complex is known, involves three different cytochromes and an Fe-S protein. In the cytochromes of these and similar complexes, the iron atom at the center of the porphyrin ring cycles between the reduced Fe (ferrous) and oxidized Fe (ferric) states. 

FIGURE 24.11 The acyl-CoA dehydrogenase reaction. The two electrons removed in this oxidation reaction are delivered to the electron transport chain in the form of reduced coenzyme Q (UQH9). 

The redox properties of quinones are crucial to the functioning of living cells, where compounds called ubiquinones act as biochemical oxidizing agents to mediate the electron-transfer processes involved in energy production. Ubiquinones, also called coenzymes Q, are components of the cells of all aerobic organisms, from the simplest bacterium to humans. They are so named because of their ubiquitous occurrence in nature. 

The body maintains an antioxidant network consisting of vitamins A, C, and E, antioxidant enzymes, and a group of related compounds called coenzyme Q, for which the general formula is shown below. The n represents the number of times that a particular group is repeated it can be 6, 8, or 10. Antioxidants are molecules that are easily oxidized, so they react readily with radicals before the radicals can react with other compounds in the body. Many common foods, such as green leafy vegetables, orange juice, and chocolate, contain antioxidants, as do coffee and tea. 

Glutaric acidurias Type I Primary defect of glutarate oxidation Type II Defect of electron transfer flavoprotein Type I Severe basal ganglia/cerebellar disease with macrocephaly. Onset 1-2 years Type II Fulminant neurological syndrome of the neonate. Often with renal/hepatic cysts. Usually fatal Diet low in lysine and tryptophan Supplementation with coenzyme Q, riboflavin, carnitine... 

Most compounds oxidized by the electron transport chain donate hydrogen to NAD+, and then NADH is reoxidized in a reaction coupled to reduction of a flavoprotein. During this transformation, sufficient energy is released to enable synthesis of ATP from ADP. The reduced flavoprotein is reoxidized via reduction of coenzyme Q subsequent redox reactions then involve cytochromes and electron transfer processes rather than hydrogen transfer. In two of these cytochrome redox reactions, there is sufficient energy release to allow ATP synthesis. In... 

It is an antioxidant vitamin. It presumably prevents oxidation of coenzyme Q and inhibits generation of peroxidation products from unsaturated fatty acids. 

Ubiquinone (also called coenzyme Q) and plasto-quinone (Fig. 10-22d, e) are isoprenoids that function as lipophilic electron carriers in the oxidation-reduction reactions that drive ATP synthesis in mitochondria and chloroplasts, respectively. Both ubiquinone and plasto-quinone can accept either one or two electrons and either one or two protons (see Fig. 19-54). 

Free energy is released as electrons are transferred along the electron transport chain from an electron donor (reducing agent or reduc-tant) to an electron acceptor (oxidizing agent or oxidant). The (electrons can be transferred in different forms, for example, as hydride ions ( FT) to NAD+, as hydrogen atoms (-H) to FMN, coenzyme Q, and FAD, or as electrons (-e ) to cytochromes. 

Correct answer = D. Thirteen of the approximately 100 polypeptides required for oxidative phosphorylation are coded for by mitochondrial DNA, including the electron transport components cytochrome c and coenzyme Q. Oxygen directly oxidizes cytochrome oxidase. Succinate dehydrogenase directly reduces FAD. Cyanide inhibits electron flow, proton pumping, and ATP synthesis. 

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