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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Haemogloblin and myoglobin enhance rat liver microsomal p-hydroxylation of aniline and acetanilide. Microsomal N-demethylation of ethylmorphine and aminopyrine is not increased by haemoproteins. 2. The enhancement of microsomal p-hydroxylation is maximal at high substrate concentration and high haeme compound concentration. 3. Detergent-purified NADPH-cytochrome c reductase, free flavins and manganese ions considerably increase the haemoglobin-mediated, tissue-free hydroxylation of aniline. Microsomal aniline hydroxylation is not enhanced by haeme, ferric ion or albumin. 4 Catalase and cyanide ions are powerful inhibitors of haemoglobin-mediated aniline hydroxylation both in the presence and absence of tissue. Carbon monoxide inhibits the hydroxylase activity of the tissue-free system to a smaller extent than that of a system containing microsomes plus haemoglobin whereas p-chloromercuribenzoate inhibits only the flavoprotein-dependent hydroxylation of aniline mediated by haemoglobin. 5. Several possibilities of interactions between substrate, microsomes and haeme compounds are proposed.
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PMID:Enhancement of microsomal aniline and acetanilide hydroxylation by haemoglobin. 82 88

Nomenclature changes of pediococci postdate the publication of Bergey's Manual. Pediococci possess both a "group" and a "type" antigen. They are gram positive, asporogenous, nonmotile, generally catalase negative, but may possess catalase-like activity. The pediococci may have either a cytochrome or a flavoprotein enzyme system. Anaerobically they are homofermentative using the PEP:PTS and the EMP pathway. Catalase positive strains utilize glucose aerobically and anaerobically while lactose and glycerol are only used aerobically. Some pentoses are fermented to lactate and acetate. Absolute requirement for folinic acid and nearly all amino acids is observed. Pediococci grow luxuriously in All Purpose Tween (APT) broth and are isolated on Rogosa SL agar. Detection can be done by electrical impedance and fluorescent antibody techniques. The Arrhenius concept was utilized in selecting metabolically efficient strains. Antibiotics, antioxidants, some chloride salts and some spices are detrimental to the pediococci. On the other hand, some chloride salts, manganese, and some spices are stimulant. Dialysis-fermentation and immobilization of pediococcal cells were recorded. Some strains decarboxylate histidine to histamine. The resting cell metabolism and the production of bacteriocin have been utilized in antibiosis. An intra and intergeneric genetic transfer system of plasmids from pediococci was by a conjugation-like mechanism. Formation of bacteriocin and fermentation of carbohydrates were linked to plasmids. Lytic bacteriophages to pediococci have not yet been identified. Industrial cultures are mainly frozen concentrates. Linear equations were developed to model the fermentative activity of pediococci and the effects of environmental factors.
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PMID:Pediococci and biotechnology. 330 17

The free-living anaerobic flagellate Hexamita sp. was observed to actively consume O2 with a K(m) O2 of 13 microM. Oxygen consumption increased linearly with O2 tension up to a threshold level of 100 microM, above which it was inhibited. Oxygen uptake was supported by a number of substrates but probably not coupled to energy conservation as cytochromes could not be detected spectro-photometrically. In addition, inhibitors specific for respiratory chain components did not significantly affect O2 uptake. Respiration was however, partially inhibited by flavoprotein and iron-sulfur protein inhibitors. NAD(P)H supported O2 consumption was measured in both particulate and soluble fractions; this activity was partially inhibited by quinacrine. A chemosensory response was observed in cells exposed to air, however no response was observed in the presence of superoxide dismutase plus catalase. Catalase and nonspecific peroxidase activity could not be detected, but superoxide dismutase plus catalase. Catalase and nonspecific peroxidase activity could not be detected, but superoxide dismutase activity was present. Superoxide dismutase was sensitive to NaN3, and H2O2 but not KCN, suggesting a Fe prosthetic group. Flow cytometric analysis revealed that thiol levels in live cells were depleted in the presence of t-butyl H2O2. The observed NADPH-driven glutathione reductase activity is believed to recycle oxidized thiols in order to re-establish reduced thiol levels in the cell. The corresponding thiol cycling enzyme glutathione peroxidase could not be detected. The ability to withstand high O2 tensions (100 microM) would enable Hexamita to spend short periods in a wider range of habitats. Prolonged exposure to O2 tensions higher than 100 microM leads to irreversible damage and cell death.
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PMID:Oxygen uptake and antioxidant responses of the free-living diplomonad Hexamita sp. 930 13

1. Brucine N-oxide was reduced by aldehyde oxidase in rabbit liver cytosol in the presence of an electron donor, 2-hydroxypyrimidine, under anaerobic conditions. The flavoprotein purified from rabbit liver exhibited significant reductase activity in the presence of electron donors. 2. Brucine N-oxide was also reduced by rabbit liver cytosol and blood in the presence of both a reduced pyridine nucleotide and FAD under anaerobic conditions. The N-oxide reductase activities were inhibited by carbon monoxide and air. However, these activities were not abolished whe n liver cytosol and blood were boiled. Rabbit erythrocytes exhibited the reductase activity, but not plasma. 3. When liver cytosol or blood was separated by DEAE-cellulose column chromatography, the fractions with the reducing activity in the presence of both NADH and FAD also showed catalase activity. 4. Catalase catalysed the brucine N-oxide reduction in the presence of both NAD(P)H and FAD. Hematin also exhibited the reductase activity in the presence of both NAD(P)H and FAD. Photochemically reduced FAD was effective in the reduction instead of NAD(P)H and FAD. 5. Bricine N-oxide reduction proceeds via two routes in liver cytosol and blood. One is enzymatic reduction by aldehyde oxidase; the other is non-enzymatic reduction catalysed by the haem group of catalase in the presence of reduced flavin.
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PMID:Enzymatic and non-enzymatic reduction of brucine N-oxide by aldehyde oxidase and catalase. 1176 40

White, D. C. (Rockefeller Institute, New York, N.Y.). Respiratory systems in hemin-requiring Haemophilus species. J. Bacteriol. 85:84-96. 1963.-If grown in Levinthal's medium or in proteose peptone medium with excess hemin, Haemophilus influenzae, H. aegyptius, and H. canis (H. haemoglobinophilus) form an electron-transport system consisting of six cytochromes and two respiratory flavoproteins. In proteose peptone, these species can greatly modify the composition of their electron-transport complex. With anaerobic incubation in the presence of nitrate, they produce increased amounts of cytochrome c(1) and the cytochrome oxidases a(1) and o. This anaerobic pattern is greatly exaggerated by growth under carbon monoxide, in which case large concentrations of cytochrome oxidase are produced. In the presence of the inhibitor secobarbital or of growth-limiting amounts of hemin, intermediate amounts of cytochromes and respiratory flavoproteins are formed. When only small amounts of hemin are present, these species grow but form no detectable cytochrome system. Catalase is the only hemoprotein found. Under these conditions, the addition of glucose induces the formation of a lactate oxidase flavoprotein if the system is incubated aerobically. This cytochromeless state also occurs when these species are grown in KCN or anaerobically without nitrate and with excess hemin. The ability of these species to modify the composition of the electron-transport system strongly suggests that this function unit is formed from individual components. Hemin-requiring Haemophilus species have a hemin-sparing compensatory mechanism that allows growth under conditions under which hemin-independent Haemophilus species will not grow.
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PMID:Respiratory systems in the hemin-requiring Haemophilus species. 1400 Feb 93

Diaphorase was studied as a possible oxidoreductase participating in NO production from some vasorelaxants. In the presence of NADH or NADPH, diaphorase can convert selected NO donors, glycerol trinitrate (GTN) and formaldoxime (FAL) to nitrites and nitrates with NO as an intermediate. This activity of diaphorase was inhibited by diphenyleneiodonium (DPI) (inhibitor of some NADPH-dependent flavoprotein oxidoreductases), while it remained uninhibited by NG-nitro-L-arginine methyl ester (inhibitor of NO synthase) 7-Ethoxyresorufin (inhibitor of cytochrome P-450 1A1 and cytochrome P-450 NADPH-dependent reductase) inhibited the conversion of GTN only. Existence of NO as an intermediate of the reaction was supported by results of electron paramagnetic resonance spectroscopy. In addition to its ability to affect the above mentioned NO donors, diaphorase was able to reduce 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) and thus to eliminate its NO scavenging effect. This activity of diaphorase could also be inhibited by DPI. The reaction of diaphorase with GTN and PTIO was not affected by superoxide dismutase (SOD) or catalase. Reaction of FAL with diaphorase was lowered with SOD by 38 % indicating the partial participation of superoxide anion probably generated by the reaction of diaphorase with NADH or NADPH. Catalase had no effect. Diaphorase could apparently be one of the enzymes participating in the metabolism of studied NO donors to NO. The easy reduction and consequent elimination of PTIO by diaphorase could affect its use as an NO scavenger in biological tissues.
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PMID:Diaphorase can metabolize some vasorelaxants to NO and eliminate NO scavenging effect of 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO). 1558 29