pH profile of cytochrome c-catalyzed tyrosine nitration.
pH profile of cytochrome c-catalyzed tyrosine nitration.
复制标题
DOI:
10.18388/abp.2006_3330
复制
发表时间:
2006
影响因子:
1.7
通讯作者:
Yasuhiro Kambayashi;Yoshiaki Hitomi;Norio Kodama;M. Kubo;Junna Okuda;Kei Takemoto;M. Shibamori;T. Takigawa;K. Ogino
中科院分区:
文献类型:
--
作者:
Yasuhiro Kambayashi;Yoshiaki Hitomi;Norio Kodama;M. Kubo;Junna Okuda;Kei Takemoto;M. Shibamori;T. Takigawa;K. Ogino
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 cytochromec-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 degrees C). The amount of nitrotyrosine formed was the greatest at pH 5. At pH 3, only cytochromec-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.