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pH Profile of cytochrome c-catalyzed tyrosine nitration

100%
Kambayashi Y., Hitomi Y., Kodama N., Kubo M., Okuda J., Takemoto K., Shibamori M., Takigawa T., Ogino K.
Acta Biochimica Polonica
|
2006
|
vol. 53
|
issue 3
577-584
EN
In the present study, we investigated how cytochrome c catalyzed the nitration of tyrosine at various pHs. The cytochrome c-catalyzed nitration of tyrosine occurred in proportion to the concentration of hydrogen peroxide, nitrite or cytochrome c. Thecytochromec-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid. These results show that the cytochrome c-catalyzednitrotyrosine formation was due to peroxidase activity. The rate constant between cytochrome c and hydrogen peroxide within the pH range of 3 - 8 was the largest at pH 6 (37°C). The amount of nitrotyrosine formed was the greatest at pH 5. At pH 3, onlycytochromec-independent nitration of tyrosine occurred in the presence of nitrite. At this pH, the UV as well as visible spectrum of cytochrome c was changed by nitrite, even in the presence of hydrogen peroxide, probably via the formation of a heme iron - nitric oxide complex. Due to this change, the peroxidase activity of cytochrome c was lost.
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Effect of Medicago sativa Mhb1gene expression on defense response of Arabidopsis thaliana plants

86%
Maassen A., Hennig J.
Acta Biochimica Polonica
|
2011
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vol. 58
|
issue 3
427-432
EN
Besides the previously described nitric oxide-detoxification activity we identified new features of class-1 non-symbiotic hemoglobin from Medicago sativa (Mhb1). Under in vitro conditions, using peroxidase in-gel activity assay, the Mhb1 protein was shown to possess also peroxidase-like activity. Due to this activity, in the presence of nitrite and hydrogen peroxide, the protein can mediate autonitration and nitration of other proteins at tyrosine residues, as revealed by tandem mass spectrometry and immune assay approaches. Mhb1 through its multifunctional activities can affect different components of signal transduction cascades operating during plant response to infections. This influence is manifested by Mhb1-mediated selective up-regulation of expression of certain pathogen inducible genes in Pseudomonas syringae infected Arabidopsis thaliana plants which overproduce Mhb1, as revealed by reverse transcription-quantitative real-time PCR analysis. Changes in expression level of these genes can influence such processes as synthesis of secondary metabolites, protein degradation and biosynthesis of ethylene. They can also result in alteration of pathogen-induced defense response of Mhb1 transgenic plants.
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