System cytochrome

Organosulfur Compounds. These compounds, Hsted in Table 8, are used in a variety of appHcations, including cooling water, paint, and metalworking. Methylenebisthiocyanate hydroly2es rapidly at a pH above 8 to cyanate ion which complexes with ferric iron to poison the cytochrome systems (36). 

Mitchell, P. (1976). Possible molecular mechanisms of the proton motive function of cytochrome systems. J. Theoret. Biol. 62. 327-367. 

The colorless sulfur-oxidizing microorganisms include relatives of the bluegreen algae (Beggiaioa and Thiothrix) and a genus of the eubac-teria (Thiobacillus). The latter require iron for growth and presumably synthesize the cytochrome systems (60). 

The cytochrome system of enzymes has long been known to be associated with the activity of the nitrifying bacteria which catalyze, for example, the oxidation of ammonia ... 

Oxidative Phosphorylation Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds. [NIH]... 

Cytochrome P-450 was also readily detectable in cunner tissue but repeated trials produced no evidence for this cytochrome system in the bivalves. 

Mirtazapine is rapidly absorbed from the gastrointestinal tract and achieves peak plasma concentrations within 2 hours of oral administration. It exhibits linear pharmacokinetics and is metabolized through the CYP450-2D6, CYP450-3A4, and, possibly, CYP450-1A2 systems (Owen and Nemeroff, 1998). Mirtazapine does not induce or inhibit any of the cytochrome systems. Only one of mirtazapine s metabolites, des-... 

Hagen, W. R. (1987). In Cytochrome Systems Molecular Biology and Bioenergetics (S. Papa, B. Chance, and L. Emster, eds.). Plenum, New York. 

The development by Chance of a dual wavelength spectrophotometer permitted easy observation of the state of oxidation or reduction of a given carrier within mitochondria.60 This technique, together with the study of specific inhibitors (some of which are indicated in Fig. 18-5 and Table 18-4), allowed some electron transport sequences to be assigned. For example, blockage with rotenone and amytal prevented reduction of the cytochrome system by NADH but allowed reduction by succinate and by other substrates having their own flavoprotein components in the chain. Artificial electron acceptors, some of which are shown in Table 18-5,... 

In a study of the inhibition of components of the cytochrome systems by maeromolecular poly-ions, Person and Fine205-20 showed that such polycations as protamine sulfate, histone, and ribonuclease inhibit the cytochrome oxidase activity of various systems. The inhibition could be reversed by the addition- of poly-ions (and, especially, by polyglucose sulfate) the latter was also shown to inhibit the oxidase system reversibly. 

Most of the numerous other riboflavin-containing enzymes contain FAD. FAD is an integral part of the biological oxidation-reduction system where it mediates the transfer of hydrogen ions from NAD11 to the oxidized cytochrome system. FAD can also accept hydrogen ions directly from a metabolite and transfer them to either NAD, a metal ion, a heme derivative, or molecular oxygen. The various mechanisms of action of FAD are probably due to differences in protein apoenzymes to which it is bound. 

Oxidation of a-amino acids to keto acids catalysed by D- and L-amino acid oxidases Oxidation of NADH via the cytochrome system catalyzed by cytochrome reductase Energy production via the TCA or Krebs cycle catalyzed by succinate dehydrogenase Fatty acid oxidation catalyzed by acyl-coenzyme A dehydrogenases Synthesis of fatty acids from acetate (80,81)... 

The reduction of UQ can be measured by the disappearance of an absorption band at 275 nm. Using this technique, it was shown that adding a substrate such as succinate caused a rapid reduction of essentially all the UQ present in the inner membrane the resulting UQH2 could be reoxidized by the cytochrome system in the presence of 02. To determine whether UQ is a necessary participant in electron transport from succinate to 02, the quinone was removed from mitochondria by selective extraction with an organic solvent. The depleted mitochondria were incapable of respiration but recovered this activity when UQ was added back. 

Reversible inhibition of cytochrome system components by macromolecular polyions, Person, P. Fine, A.S. Arch. Biochem. Biophys. 1961, 94, 392. 

Macroion interactions involving components of cytochrome system 5. Reduction of cytochrome c by synthetic polysaccharides, Mora, P.T. Creskoff, E.L. Person, P. J. Biol. Chem. 1967, 242, 1280. 

Demin, V.I., Androsova, I.M. and Ozemyuk, N.D. (1989). Energy metabolism adaptations in fish the influence of swimming speed and temperature on the cytochrome system of skeletal muscle (In Russian). Doklady Akademii Nauk SSSR 308,241-246. 

Verzhbinskaya, N.A. (1953). Cytochrome system of the brain in phylogenesis of vertebrates (In Russian). Physiologicheskii Zhumal, SSSR 39,17-20. 

Note also that chemical reactions accompanied by water formation are always thermodynamically profitable. Therefore, H+ ion participation in water formation during the ADP phosphorylation process makes this reaction much simpler. On the other hand, the water formed is bound to the / j factor. It is common knowledge that the reaction is intensified by water-binding compounds. Then water is dissociated to ions, emitted to different sides of the membrane, and this process is synchronized with ATP desorption. Desorbed protons are localized at H+-ATP-synthase, directly at the cytochrome system of the respiratory chain. Therefore, they quickly interact with activated oxygen, producing water at the final stage of respiration (3.50). 

Keilin, D., and Hartree, E. F. (1947). Activity of the Cytochrome System in Heart Muscle Preparations. Biochem J 41 500. 

The production of even small amounts of hydrogen sulfide by sulfate reducers can have a marked effect on populations within a habitat. Since it is extremely toxic to aerobic organisms because of its affinity for Fe in the cytochrome systems, hydrogen sulfide can kill for example nematodes and plants. 

Lawrle, R. A. (1953) The activity of the cytochrome system In muscle and Its relation to myoglobin. Blochem. J. 55 298-305. Lawrle, R. A. (1953) Effect of enforced exercise on myoglobin concentration In muscle. Nature London. 171 1069-71. John-Alder, H. (1984) Seasonal variations In activity, aerobic energetic capacities, and plasma thyroid hormones (T3 and T4)... 

Link, T. A., Sch%ogger, H., and Von Jagow, G., 1987, Structural analysis of the bpcomplex from beef heart mitochondria by the sidedness hydropathy plot and by comparison with other be complexes, in Cytochrome Systems Molecular Biology and Bioenergetics, (S. Papa, B. Chance, and L. Emster, eds.) Plenum Press, New York, pp. 289n301. 

Photons are able to cause such effects. Light sensitivity of cytochrome containing systems has been known for a long time. For example, when bacteria of the type Rhodomicrobium (red microbe) were exposed to near infrared (NIR) radiation, their cytochrome system was oxidized from the ferrous to the ferric state (30). It is important to note that an archaic type of anoxygenic photosynthesis based on the oxidation of Fe(II) species has in the mean time been discovered (31), and that Rhodomicrobium strains are now known to belong to such types of photoferrotrophic microorganisms (32). 

Azoxystrobin or Methyl (E)-2- 2-(6-(2-cyanophen oxy) pyrimidin-4-yloxy]phenyl -3-methoxyacrylate Strobilurin respiration by blocking electron transfer between cytochromes, systemic with protective action Control of a wide range of pathogens on cereals, vines, potato, rice, fiuits, nuts, and so on 11-32... 

There is one bacterial system where such reversed electron transfer is of great importance. In Rps. sphaeroides the generated by cyclic electron flow through the reaction centre and cytochrome system is used to induce reversed electron flow from the level of the ubiquinone pool to the NADH/NAD" pool, in a manner analogous to that described for mitochondria. The role of this is to supply low potential electrons for the biosynthetic functions of the cell [38]. 

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