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Flavohemoglobin and nitric oxide detoxification in the human protozoan parasite Giardia intestinalis.
Flavohemoglobins (flavoHbs), commonly found in bacteria and fungi, afford protection from nitrosative stress by degrading nitric oxide (NO) to nitrate. Giardia intestinalis, a microaerophilicExpand
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Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species.
The functional role of mitochondria in cell physiology has previously centered around metabolism, with oxidative phosphorylation playing a pivotal role. Recently, however, this perspective hasExpand
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Trichomonas vaginalis degrades nitric oxide and expresses a flavorubredoxin-like protein: a new pathogenic mechanism?
Besides possessing many physiological roles, nitric oxide (NO) produced by the immune system in infectious diseases has antimicrobial effects. Trichomoniasis, the most widespread non-viral sexuallyExpand
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Cytochrome bd oxidase and nitric oxide: From reaction mechanisms to bacterial physiology
Experimental evidence suggests that the prokaryotic respiratory cytochrome bd quinol oxidase is responsible for both bioenergetic functions and bacterial adaptation to different stress conditions.Expand
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Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes.
The therapeutic use of cell-free haemoglobin as a blood substitute has been hampered by toxicological effects. A model asolectin (phosphatidylcholine/phosphatidylethanolamine) liposome system wasExpand
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Intermediates in the catalytic cycle of lentil (Lens esculenta) seedling copper-containing amine oxidase.
Spectrophotometry and rapid-scanning stopped-flow spectroscopy have been used to investigate the visible absorbance changes that occur in the course of the reduction of lentil (Lens esculenta)Expand
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Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress
Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b 558, b 595 and d. We found that the enzyme, as‐prepared or in turnover with O2, rapidly decomposes H2O2 with formation ofExpand
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The oxidation of cytochrome-c oxidase vesicles by hemoglobin.
Human hemoglobin has been used as a pro-oxidant for artificial unilamellar phospholipid vesicles, containing cytochrome-c oxidase inserted into the bilayer. This experimental system was suitable toExpand
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Respiratory control in cytochrome oxidase vesicles is correlated with the rate of internal electron transfer.
Cytochrome c oxidase, after reconstitution into phospholipid vesicles, displays respiratory control. This appears as an inhibition of substrate oxidation (cytochrome c) or reduction (O2) rates which,Expand
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