Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of hyperbaric oxygen (1--5 ata for 1 hr) on the activity of cytochrome oxidase, peroxidase, lipid content and phagocytic activity of neutrophils was studied. The dynamics of the recovery of those parameters was followed. A multimodal relationship between the pressure level and changes in the enzyme activity and lipid content was noted. The decrease in the activity of peroxidase was more pronounced than that of cytochrome oxidase in all cases. The dynamics of the recovery of the above parameters was shown to depend on the pressure level. The cytochemical parameters returned to the normal within 24 hours. The decline in the activity of cytochrome oxidase, peroxidase and in the lipid content of peripheral neutrophils was followed by a decrease in the phagocytic activity. These changes were closely correlated.
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PMID:[Action of oxygen under increased pressure on the neutrophil metabolism in the peripheral blood]. 22 25

The effect of curantil on the values of energy metabolism in different parts of the myocardium was studied on dogs with experimental myocardial infarction. Tissue respiration, the activity of Krebs' cycle enzymes, cytochrome oxidase, pentose phosphate cycle and glycolysis, and the content of glycogen and adenyl components were studied. It was established that curantil has a positive effect on energy processes, particularly in myocardial areas not involved in ischemia. It is suggested that activation of tissue oxidation enzymes, which improves oxygen utilization and increases ATP production, is among the mechanisms of the curantil effect. It is noted that curantil stimulates the synthesis of glycogen and inhibits its decomposition. The accumulation in the myocardium of AMP, the precursor of adenosine possessing a marked coronarolytic effect, is an important aspect of the drug's action.
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PMID:[Metabolic shifts in acute period of myocardial infarct and the possibility of their correction with curantil]. 22 32

1. In the absence of cytochrome c, ferrocyanide or ferrous sulphate reduces cytochrome c oxidase (EC 1.9.3.1), but no continuous oxygen uptake ensues, as it does with N,N,N',N'-tetramethyl-p-phenylenediamine or reduced phenazine methosulphate as reductants, unless a substoichiometric amount of cytochrome c or an excess of clupein is present. Cytochrome c cannot be replaced by porphyrin cytochrome c. 2. Cytochrome c, porphyrin cytochrome c and clupein all stimulate the reduction of cytochrome aa3 by ferrocyanide. 3. A model is proposed to explain these findings in which a high-affinity site for cytochrome c on the oxidase regulates the access of hydrophilic electron donors to a low-affinity site, and reduction via the high-affinity site is required for continuous oxygen uptake. 4. Furthermore, it is shown that upon reaction of oxidase with ferrocyanide, cyano-oxidase is formed.
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PMID:Ferrocyanide as electron donor to cytochrome aa3. Cytochrome c requirement for oxygen uptake. 22 35

An increase in activity of several dehydrogenases of tricarboxylic acid cycle (NADP-dependent malate dehydrogenase, alpha-ketoglutarate dehydrogenase) was observed in rat liver tissue under conditions of acute hemorrhage. The enzymatic activity was slightly higher in the group of animals with relatively prolonged life-time as compared with those, which lived less than 4 hrs. Activity of cytochrome oxidase was inhilited in the both groups of animals (by 27% and 29%, respectively). The less distinct decrease in both temperature in the group of animals with prolonged life-time might maintain the rate of Krebs cycle substrates oxidation. Activation of respiration in liver tissue under conditions of the hemorrhage is considered as a compensatory reaction tending to improve oxygen utilization in hypoxia. At the same time, inhibition oy cytochrome oxidase demonstrates the impairment of electron transport and decreased rate of energy production in liver mitochondria.
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PMID:[Tissue respiratory enzymes in the rat liver in acute blood loss]. 22 69

1. In the presence of both CO and O2, ox heart cytochrome c oxidase forms a 607 nm-peak intermediate distinct from both the cytochrome a2+a3 2+CO and the cytochrome a3+a3 2+CO ('mixed-valence') CO complexes. 2. This aerobic CO compound is stable towards ferricyanide addition, but decomposed on treatment with ferric cytochrome a2 ligands such as formate, cyanide and azide. 3. Addition of formate or cyanves rise to a complex with alpha-peak at 598 nm, not identical with any azide complex of the free enzyme, but possibly a cytochrome a3 2+NO complex produced by oxidative attack of partially reduced O2 on the azide. 4. The results support the idea that although the initial reaction of oxygen is with cytochrome a3 2+, the next step is not an oxidation of the ferrous cytochrome a3, but a transfer of O2 to a neighbouring group, such as Cu+, to give Cu2+O2- or similar complexes. 5. The aerobic CO complex is then identified as a3+a3 2+COCu2+O2-; a similar compound ('Compound C') is formed by photolysis of a3+a3 2+CO (the 'mixed-valence' CO complex) in the presence of oxygen at low temperatures.
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PMID:Effects of inhibitory ligands on the aerobic carbon monoxide complex of cytochrome c oxidase. 23 68

Virulent Treponema pallidum has been shown to survive in KCN-containing artificial medium. Oxygen uptake being sensitive to cyanide, the observation indicates that treponemes do not have a cytochrome oxidase system. KCN had a killing effect only at a 15--30 mM final concentration. The data show that the Budapest strain of T. pallidum is an anaerobic organism.
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PMID:Effect of KCN on the motility of Treponema pallidium. 23 17

1. Tissue oxygen uptake and enzyme activities were investigated in the naked mole rat, Heterocephalus glaber, a mammal notable for its low body temperature and metabolism and poor temperature regulating ability. 2. Q10 for O2 uptake of Heterocephalus crude liver homogenates ranged from 1.91 for the temperature interval 25-30 degrees C to 1.76 within the range 30-38 degrees C, values similar to those reported for typical homoiotherms. 3. Km pyruvate of lactate dehydrogenase in heart muscle had the same temperature dependence in the mole rat and mouse. 4. O2 uptake and cytochrome oxidase activity of skeletal muscle were higher for mole rat than mouse. The reverse was true for heart muscle. Brain and liver O2 uptake showed similar values for both species, while kidney O2 uptake was highest in the mouse. 5. Pyruvate kinase activity in heart and skeletal muscle was higher in mouse than mole rat, suggesting a greater reliance on glycolysis in the former. 6. Na+, K+ -ATPase activity of liver and kidney was 60% higher in mouse than mole rat, while brain was 30% higher in mouse. 7. The results indicate that the effects of temperature on tissue metabolism in the mole rat conform to those in typical homoiotherms. The low body temperature and O2 uptake in the mole rat find no expression in the tissue respiratory capacity.
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PMID:Tissue metabolism and enzyme activities in the rodent Heterocephalus glaber, a poor temperature regulator. 23 74

1. The relationship between chain composition and the efficiency of respiration-linked proton translocation was studied in nine bacterial species of widely differing taxonomic and ecological status. 2. All the bacteria investigated contained respiratory chain dehydrogenases, ubiquinone and/or menaquinone, cytochrome b and cytochrome oxidase aa3 and/or o. In addition, some of these organisms also contained pyridine nucleotide transhydrogenase and/or cytochrome c. 3. leads to H+/O ratios of whole cell suspensions oxidising endogenous substrates were in the approximate range 4-8 mol H+ translocated per g-atom oxygen consumed. It was concluded from the observed leads to H+/O ratios of cells loaded with specific substrates that proton-translocating loops 1 and 2 were present in all of the organisms investigated, but that loops 0 and 3 were dependent upon the presence of pyridine nucleotide transhydrogenase and cytochrome c respectively. 4. The wide range in energy conservation efficiency which was observed in these organisms is discussed in relation to their respiratory chain composition and natural habitat.
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PMID:Bacterial respiration-linked proton translocation and its relationship to respiratory-chain composition. 24 Jun 79

The oxidation-reduction potentials of Escherichia coli cytochromes have been studied by a recently described technique for automated electrodic potentiometry (Hendler, R.W., Songco, D., and Clem, T.R. (1977) Anal. Chem. 49, 1908-1913; Hendler, R.W. (1977) Anal. Chem. 49, 1914-1918), where entire spectra are recorded at a series of solution potentials. New techniques for resolution of the spectra versus voltage data have been applied. The results indicate that a 1-electron transport chain conducts electrons from substrate to cytochrome d, which is the cytochrome oxidase. Cytochrome d contains several components which appear to increase electron transfer first to a 2-electron stage and then to a 4-electron stage for the final reduction of a molecule of oxygen to 2 molecules of water.
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PMID:Potentiometric analysis of Escherichia coli cytochromes in the optical absorbance range of 500 nm to 700 nm. 38 69

1. The reactions of cytochrome omicron in intact cells of aerobically grown Escherichia coli with O2 and CO have been studied at low temperature. 2. Flash photolysis of CO-liganded cells in the presence of O2 and at temperatures between -79 and -102 degrees C results in the oxidation of kinetically heterogeneous beta-type cytochromes (including cytochrome omicron), but not of cytochrome d. 3. The reaction of reduced cytochrome omicron with O2 involves O2 binding to give intermediate(s) with spectral characteristics similar to that of the reduced oxidase-CO complex. Observation in the alpha-region suggests that unexplained ligand dissociation accompanies the initial O2 binding. 4. At temperatures below -98 degrees C, an 'end point' in the reaction is reached; further reaction and oxidation of cytochrome omicron occurs on raising the temperature. 5. There is a linear relationship between the rate of formation of the oxygen compound and the O2 concentration up to 0.5 mM. The second-order constant for its formation (k+1) is 0.91 M-1.S-1 at -101 degrees C. The reaction is not readily reversible, the value of k-1 being 1.4 X 10(-5) S-1 and the kd 1.5 X 10(-5) M. 6. The energy of activation for this reaction at low temperatures is 29.9kJ (7.1 kcal)/mol. 7. The reaction with O2 is distinguished from that with CO by the markedly lower velocity and high photolytic reversibility of the latter. 8. Comparisons are drawn between the intermediate(s) in the O2 reaction of cytochrome omicron in E. coli and those identified in other bacteria and in the reaction of cytochrome aa3 with O2.
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PMID:The reaction of cytochrome omicron in Escherichia coli with oxygen. Low-temperature kinetic and spectral studies. 39 55


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