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Mitochondria inner membrane

The marker enzymes used in this experiment are as follows vanadate-sensitive H+-ATPase (plasma membrane), nitrate-sensitive H+-ATPase or pyrophosphatase (tonoplast), TritonX-100 stimulated-UDPase or IDPase (Golgi complex), antimycin A-insensitive NADPH cytochrome c reductase (ER), and cytochrome c oxidase (mitochondria inner membrane). NADH cytochrome c reductase activity is found to be 10 times higher than NADPH cytochrome c reductase activity. Chlorophyll content can be measured as the chloroplast marker. The chlorophyll content is calculated by the following equation. Before measurement, auto zero is performed at 750 ran. [Pg.164]

Electron transport systems perform important functions concerning respiration and energy metabolism in eucaryotes [22, 23], The electron transport reactions occur at the mitochondria inner membrane formed by electron transport proteins [24] and the lipid bilayer built up by the self-assembly of phospholipids as vital smfactants [25, 26]. The electron transport proteins include redox catalysts such as nicotinamide, iron [27, 28], and quinones [29]. The electrons produced by these redox reactions transfer through the lipid bilayer. While the relationship between the electron transport mechanisms and the molecular self-assembly in vivo has been clarified, control of the self-assembly by electron transport has been applied for an artificial polymeric surfactant. [Pg.1]

Fatty acid" Plasmalemma" Whole organelles Mitochondria Inner membranes 1 Outer membranes Peroxisomes Microsomes ... [Pg.286]

Up to 35% of beef-heart mitochondria inner membrane structural protein obtained either by the method of Griddle et al. (1962) or that of S. H. Richardson et al. (1964) has been shown to be denatured ATPase (Schatz and Saltzgaber, 1969). The ratio of structural protein to lipids is thus as low as 0.65. [Pg.167]

Because both oxidative and photophosphorylation occur at large sub-entities in organelles of heterotrophic and autotrophic cell, the plasma membrane, the mitochondria inner membrane or the chloroplast thylakoid system, and in a cooperative fashion - one thylakoid contains about 10 CF CF complexes -, in reconstitution experiments the danger of misinterpretation is always inherent The reappearence of catalytic activity of the membrane system may be due to "structural reconstitution", i.e. repair of H leakeness by the added soluble component (Schatz et al., 1967, McCarty, Racker, 1967). [Pg.571]

An electrophoresis gel of the bovine heart complex is shown in Figure 21.14. The total mass of the protein in the complex, composed of 13 subunits, is 204 kD. Subunits I through III, the largest ones, are encoded by mitochondrial DNA, synthesized in the mitochondrion, and inserted into the inner membrane from the matrix side. The smaller subunits are coded by nuclear DNA and synthesized in the cytosol. [Pg.689]

The link with the final electron acceptor, O2, is the enzyme cytochrome c oxidase which spans the inner membrane of the mitochondrion. It consists of cytochromes a and a3 along with two, or possibly three, Cu atoms. The details of its action are not fully established but the overall reaction catalysed by the enzyme is ... [Pg.1101]

The mitochondrion has an outer and an inner membrane (Figure 1). The outer membrane contains pores formed from a protein, porin, which allow exchange of molecules with molecular weights up to about 2,000 between the cytosol and the intermembrane space. The inner membrane is extensively invaginated to increase its surface area. It has a different lipid composition from the outer membrane and is rich in the acidic phospholipid cardiolipin (diphosphatidyl-glycerol) which is only found in animal cells in mitochondria. Cardiolipin confers good electrical insulating properties on the inner membrane which is impermeable... [Pg.108]

A few patients have been described with a defect involving the carnitine-acylcarnitine translocase system, which facilitates the movement of long-chain acylcarnitine esters across the inner membrane of the mitochondrion (Fig. 42-2). These patients have extremely low carnitine concentrations and minimal dicarboxylic aciduria [4]. [Pg.701]

Mitochondria are distinct organelles with two membranes. The outer membrane limits the organelle and the inner membrane is thrown into folds or shelves that project inward and are called cristae mitochondriales. The uptake of most mitochondrion-selective dyes is dependent on the mitochondrial membrane potential. Conventional fluorescent stains for mitochondria, such as rhodamine and tetramethylrosamine, are readily sequestered by functioning mitochondria. They are, however, subsequently washed out of the cells once the mitochondrion s membrane potential is lost. This characteristic limits their use in experiments in which cells must be treated with aldehyde-based fixatives or other agents that affect the energetic state of the mitochondria. To overcome this limitation, the research... [Pg.87]

The sequence of the carriers in the chain is shown in Figure 9.6. Each of the components of the chain reduces the next, in sequence, according to the redox potential (Table 9.3). The enzymes and their prosthetic groups are organised into complexes, which can be isolated by gentle disruption of the whole mitochondrion or its inner membrane. Ubiqui-... [Pg.184]

Figure 9.13 Examples of mitochondrial transport systems for anions. 0 The anb port system transfers malate into but oxo-glutarate out of the mitochondrion. The symport system transfers both pyruvate and protons into the mitochondrion across the inner membrane. Both transport processes are electroneutral. Figure 9.13 Examples of mitochondrial transport systems for anions. 0 The anb port system transfers malate into but oxo-glutarate out of the mitochondrion. The symport system transfers both pyruvate and protons into the mitochondrion across the inner membrane. Both transport processes are electroneutral.
Figure 11.3 Mechanism of transfer of acetyl-CoA out of the mitochondrion. In the mitochondrion, acetyl-CoA reacts with oxaloacetate to form citrate, which is transported across the mitochondrial inner membrane. In the cytosol, citrate is split to re-form citrate and oxaloacetate, catalysed by citrate lyase. It has been shown that inhibition of citrate lyase inhibits fatty acid synthesis. Figure 11.3 Mechanism of transfer of acetyl-CoA out of the mitochondrion. In the mitochondrion, acetyl-CoA reacts with oxaloacetate to form citrate, which is transported across the mitochondrial inner membrane. In the cytosol, citrate is split to re-form citrate and oxaloacetate, catalysed by citrate lyase. It has been shown that inhibition of citrate lyase inhibits fatty acid synthesis.
As mentioned, although complexes I through V are all integrated into the inner membrane of the mitochondrion, they are not usually in contact with one another, since the electrons are transferred by ubiquinone and cytochrome c. With its long apolar side chain, ubiquinone is freely mobile within the membrane. Cytochrome c is water-soluble and is located on the outside of the inner membrane. [Pg.140]

Oxidizible substrates from glycolysis, fatty acid or protein catabolism enter the mitochondrion in the form of acetyl-CoA, or as other intermediaries of the Krebs cycle, which resides within the mitochondrial matrix. Reducing equivalents in the form of NADH and FADH pass electrons to complex I (NADH-ubiquinone oxidore-ductase) or complex II (succinate dehydrogenase) of the electron transport chain, respectively. Electrons pass from complex I and II to complex III (ubiquinol-cyto-chrome c oxidoreductase) and then to complex IV (cytochrome c oxidase) which accumulates four electrons and then tetravalently reduces O2 to water. Protons are pumped into the inner membrane space at complexes I, II and IV and then diffuse down their concentration gradient through complex V (FoFi-ATPase), where their potential energy is captured in the form of ATP. In this way, ATP formation is coupled to electron transport and the formation of water, a process termed oxidative phosphorylation (OXPHOS). [Pg.357]

Fig. 7.3.1 The heme synthesis pathway starts in the mitochondrion. The next four steps proceed in the cytosol. Coproporphyrinogen oxidase is in the intermembrane space of the mitochondrion, and the last two enzymes reside at the mitochondral matrix side of the inner membrane. The product heme represses the first and rate-limiting enzyme -aminolevulinic acid (5-ALA) synthase at transcription, during the translation step, and by its transport into the mitochondrion... [Pg.755]

FIGURE 19-1 Biochemical anatomy of a mitochondrion. The convolutions (cristae) of the inner membrane provide a very large surface area. The inner membrane of a single liver mitochondrion may have more than 10,000 sets of electron-transfer systems (respiratory chains) and ATP synthase molecules, distributed over the membrane surface. Heart mitochondria, which have more profuse cristae and thus a much larger area of inner membrane, contain more than three times as many sets of electron-transfer systems as liver mitochondria. The mitochondrial pool of coenzymes and intermediates is functionally separate from the cytosolic pool. The mitochondria of invertebrates, plants, and microbial eukaryotes are similar to those shown here, but with much variation in size, shape, and degree of convolution of the inner membrane. [Pg.691]

How Many Protons in a Mitochondrion Electron transfer translocates protons from the mitochondrial matrix to the external medium, establishing a pH gradient across the inner membrane (outside more acidic than inside). The tendency of protons to diffuse back into the matrix is the driving force for ATP synthesis by ATP synthase. During oxidative phosphorylation by a suspension of mitochondria in a medium of pH 7.4, the pH of the matrix has been measured as 7.7. [Pg.749]

Structure of the mitochondrion The components of the electron transport chain are located in the inner membrane. Although the outer membrane contains special pores, making it freely perme-... [Pg.73]

Structure of a mitochondrion showing schematic representation of the electron transport chain and ATP synthesizing structures on the inner membrane. mtDNA = mitochondrial DNA mtRNA = mitochondrial RNA. [Pg.74]

What are the molar concentrations of the electron carriers in mitochondrial membranes In one experiment, cytochrome b was found in rat liver mitochondria to the extent of 0.28 pmol/g of protein. If we take a total mitochondrion as about 22% protein, the average concentration of the cytochrome would be 0.06 mM. Since all the cytochromes are concentrated in the inner membranes, which may account for 10% or less of the volume of the mitochondrion, the concentration of cytochromes may approach 1 mM in these membranes. This is sufficient to ensure rapid reactions with substrates. [Pg.1019]

Mitochondria are intracellular centers for aerobic metabolism. They are cell organelles that are identified by well-defined structural and biochemical properties. In morphological terms, mitochondria are relatively large particles that are characterized by the presence of two membranes, a smooth outer membrane that is permeable to most important metabolites and an inner membrane that has unique transport properties. The inner membrane is highly folded, which serves to increase its surface area. Figure E10.1, which shows the structure of a typical mitochondrion, divides the organelle into four major components inner membrane, outer membrane, intermembrane space, and the matrix. These regions are associated with different and... [Pg.357]

In eukaryotes, most of the reactions of aerobic energy metabolism occur in mitochondria. An inner membrane separates the mitochondrion into two spaces the internal matrix space and the intermembrane space. An electron-transport system in the inner membrane oxidizes NADH and succinate at the expense of 02, generating ATP in the process. The operation of the respiratory chain and its coupling to ATP synthesis can be summarized as follows ... [Pg.327]


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