Abstract
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. The cytochrome c-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid. These results show that the cytochrome c-catalyzed nitrotyrosine 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, only cytochrome c-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.
| Original language | English |
|---|---|
| Pages (from-to) | 577-584 |
| Number of pages | 8 |
| Journal | Acta Biochimica Polonica |
| Volume | 53 |
| Issue number | 3 |
| Publication status | Published - 2006 |
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Keywords
- Cytochrome c
- Nitrite
- Nitrotyrosine
- pH
- Pseudo-peroxidase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
pH profile of cytochrome c-catalyzed tyrosine nitration. / Kambayashi, Yasuhiro; Hitomi, Yoshiaki; Kodama, Norio; Kubo, Masayuki; Okuda, Junna; Takemoto, Kei; Shibamori, Masafumi; Takigawa, Tomoko; Ogino, Keiki.
In: Acta Biochimica Polonica, Vol. 53, No. 3, 2006, p. 577-584.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - pH profile of cytochrome c-catalyzed tyrosine nitration
AU - Kambayashi, Yasuhiro
AU - Hitomi, Yoshiaki
AU - Kodama, Norio
AU - Kubo, Masayuki
AU - Okuda, Junna
AU - Takemoto, Kei
AU - Shibamori, Masafumi
AU - Takigawa, Tomoko
AU - Ogino, Keiki
PY - 2006
Y1 - 2006
N2 - 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. The cytochrome c-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid. These results show that the cytochrome c-catalyzed nitrotyrosine 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, only cytochrome c-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.
AB - 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. The cytochrome c-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid. These results show that the cytochrome c-catalyzed nitrotyrosine 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, only cytochrome c-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.
KW - Cytochrome c
KW - Nitrite
KW - Nitrotyrosine
KW - pH
KW - Pseudo-peroxidase
UR - http://www.scopus.com/inward/record.url?scp=33749835014&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33749835014&partnerID=8YFLogxK
M3 - Article
C2 - 16951741
AN - SCOPUS:33749835014
VL - 53
SP - 577
EP - 584
JO - Acta Biochimica Polonica
JF - Acta Biochimica Polonica
SN - 0001-527X
IS - 3
ER -