Respiratory chain oxygen transport

As components in the respiratory chain of electron transport from substrate to oxygen (Figure 12-3). 

Most of the energy liberated during the oxidation of carbohydrate, fatty acids, and amino acids is made available within mitochondria as reducing equivalents (—H or electrons) (Figure 12-2). Mitochondria contain the respiratory chain, which collects and transports reducing equivalents directing them to their final reaction with oxygen to form water, the machinery for... 

The respiratory chain is one of the pathways involved in oxidative phosphorylation (see p. 122). It catalyzes the steps by which electrons are transported from NADH+H or reduced ubiquinone (QH2) to molecular oxygen. Due to the wide difference between the redox potentials of the donor (NADH+H or QH2) and the acceptor (O2), this reaction is strongly exergonic (see p. 18). Most of the energy released is used to establish a proton gradient across the inner mitochondrial membrane (see p. 126), which is then ultimately used to synthesize ATP with the help of ATP synthase. 

In order to carry out all of these different functions, peroxisomes are equipped with a unique set of enzyme proteins, catalysing the different reactions involved. In addition, the peroxisomal membrane contains specific transporters in order to take up substrates from the cytosol and release the end products of peroxisomal metabolism. Since peroxisomes lack a citric acid cycle as well as a respiratory chain, the end products of peroxisomal metabolism, such as acetyl-CoA, propionyl-CoA and a range of other acyl-Co A esters predominantly derived from fatty acid beta-oxidation, are exported from the peroxisomal interior and shuttled to mitochondria for full oxidation to C02 and H20. The same applies to the NADH produced during beta-oxidation, which is reoxidised via redox-shuttles so that the NADH generated in peroxisomes is ultimately reoxidised in the mitochondrial respiratory chain at the expense of molecular oxygen. 

The inner mitochondrial membrane can be disrupted into five sepa rate enzyme complexes, called complexes I, II, III, IV, and V. Complexes I to IV each contain part of the electron transport chain (Figure 6.8), whereas complex V catalyzes ATP synthesis (see p. 78). Each complex accepts or donates electrons to relatively mobile electron carriers, such as coenzyme Q and cytochrome c. Each car rier in the electron transport chain can receive electrons from an electron donor, and can subsequently donate electrons to the next carrier in the chain. The electrons ultimately combine with oxygen and protons to form water. This requirement for oxygen makes the electron transport process the respiratory chain, which accounts for the greatest portion of the body s use of oxygen. 

Keilin soon realized that three of the absorption bands, those at 604,564, and 550 nm (a, b, and c), represented different pigments, while the one at 521 nm was common to all three. Keilin proposed the names cytochromes a, b, and c. The idea of an electron transport or respiratory chain followed6 quickly as the flavin and pyridine nucleotide coenzymes were recognized to play their role at the dehydrogenase level. Hydrogen removed from substrates by these carriers could be used to oxidize reduced cytochromes. The latter would be oxidized by oxygen under the influence of cytochrome oxidase. 

In juvenile liver fluke and miracidia, a respiratory chain up to cytochrome c oxidase is active and all evidence obtained so far indicates that in F. hepatica at least this electron-transport chain is not different from the classical one present in mammalian mitochondria (Figs 20.1 and 20.2). In the aerobically functioning stages, electrons are transferred from NADH and succinate to ubiquinone via complex I and II of the respiratory chain, respectively. Subsequently, these electrons are transferred from the formed ubiquinol to oxygen via the complexes III and IV of the respiratory chain. 

The fermentation tests were carried out in shake flasks, STR and FBR. The effect of the following parameters was investigated the amount of gel and the total cell concentration in the bioreactor the addition of hydrogen acceptor (acetone), instead of air, to activate the electron transport in the respiratory chain and the use of Teflon-made filters as air diffusers to reduce air bubble dimension and increase oxygen solubility. 

It is already known that under anaerobic conditions the xylose-fermenting yeasts do not produce ethanol because the electron transport in the respiratory chain is not activated (20). Since either aeration or oxidizing compounds, such as acetone, could increase the ethanol yield, the effect of improving the oxygenation of the medium or adding oxidizers was investigated using an STR partially filled with marbles. 

There are two fermentative processes that at first appear to be quite similar to oxygen and nitrate-dependent respirations the reduction of C02 to methane and of sulfate to sulfide. However, on closer examination, it is clear that they bear little resemblance to the process of denitrification. In the first place, the reduction of C02 and of sulfate is carried out by strict anaerobes, whereas nitrate reduction is carried out by aerobes only if oxygen is unavailable. Equally important, nitrate respirers contain a true respiratory chain sulfate and C02 reducers do not. Furthermore, the energetics of these processes are very different. Whereas the free energy changes of 02 and nitrate reduction are about the same, the values are much lower for C02 and sulfate reduction. In fact, the values are so low that the formation of one ATP per H2 or NADH oxidized cannot be expected. Consequently, not all the reduction steps in methane and sulfide formation can be coupled to ATP synthesis. Only the reduction of one or two intermediates may yield ATP by electron transport phosphorylation, and the ATP gain is therefore small, as is typical of fermentative reactions. 

Figure 7-1. Pathways of fuel metabolism and oxidative phosphorylation. Pyruvate may be reduced to lactate in the cytoplasm or may be transported into the mitochondria for anabolic reactions, such as gluconeogenesis, or for oxidation to acetyl-CoA by the pyruvate dehydrogenase complex (PDC). Long-chain fatty acids are transported into mitochondria, where they undergo [ -oxidation to ketone bodies (liver) or to acetyl-CoA (liver and other tissues). Reducing equivalents (NADH, FADII2) are generated by reactions catalyzed by the PDC and the tricarboxylic acid (TCA) cycle and donate electrons (e ) that enter the respiratory chain at NADH ubiquinone oxidoreductase (Complex 0 or at succinate ubiquinone oxidoreductase (Complex ID- Cytochrome c oxidase (Complex IV) catalyzes the reduction of molecular oxygen to water, and ATP synthase (Complex V) generates ATP fromADP Reprinted with permission from Stacpoole et al. (1997).

Cytochrome c, a small heme protein (mol wt 12,400) is an important member of the mitochondrial respiratory chain. In this chain it assists in the transport of electrons from organic substrates to oxygen. In the course of this electron transport the iron atom of the cytochrome is alternately oxidized and reduced. Oxidation-reduction reactions are thus intimately related to the function of cytochrome c, and its electron transfer reactions have therefore been extensively studied. The reagents used to probe its redox activity range from hydrated electrons (I, 2, 3) and hydrogen atoms (4) to the complicated oxidase (5, 6, 7, 8) and reductase (9, 10, 11) systems. This chapter is concerned with the reactions of cytochrome c with transition metal complexes and metalloproteins and with the electron transfer mechanisms implicated by these studies. 

The electron-transport chain, or respiratory chain in mitochondria forms the means by which electrons, from the reduced electron carriers of intermediary metabolism, are channeled to oxygen and protons to yield H2O. The main components of the chain are as follows. 

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