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Three distinct Arabidopsis hemoglobins exhibit peroxidase‐like activity and differentially mediate nitrite‐dependent protein nitration
Author(s) -
Sakamoto Atsushi,
Sakurao Sho-hei,
Fukunaga Keiko,
Matsubara Toshiyuki,
Ueda-Hashimoto Manami,
Tsukamoto Shigefumi,
Takahashi Misa,
Morikawa Hiromichi
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.005
Subject(s) - nitrite , peroxidase , arabidopsis , biochemistry , hydrogen peroxide , chemistry , nitrite reductase , hemoglobin , nitration , heme , arabidopsis thaliana , reactive nitrogen species , hemeprotein , reactive oxygen species , enzyme , nitrate , organic chemistry , gene , mutant
All plants examined to date possess non‐symbiotic hemoglobin whose physiological role remains unclear. The present study explored the catalytic function of three representative classes of the plant hemoglobin from Arabidopsis thaliana : AtGLB1, AtGLB2, and AtGLB3. Purified recombinant proteins of these hemoglobins displayed hydrogen peroxide‐dependent oxidation of several peroxidase substrates that was sensitive to cyanide, revealing intrinsic peroxidase‐like activity. In the presence of nitrite and hydrogen peroxide, AtGLB1 was the most efficient at mediating tyrosine nitration of its own and other proteins via the formation of reactive nitrogen species as a result of nitrite oxidation. AtGLB1 mRNA significantly accumulated in Arabidopsis seedlings exposed to nitrite, supporting the physiological relevance of its function to nitrite and nitrite‐derived reactive nitrogen species.