Three distinct Arabidopsis hemoglobins exhibit peroxidase-like activity and differentially mediate nitrite-dependent protein nitration
Three distinct Arabidopsis hemoglobins exhibit peroxidase-like activity and differentially mediate nitrite-dependent protein nitration
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DOI：
10.1016/j.febslet.2004.07.005
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发表时间：
2004-08-13
期刊：
影响因子：
3.5
通讯作者：
Morikawa, H
中科院分区：
文献类型：
--
作者：
Sakamoto, A;Sakurao, S;Morikawa, H
迄今为止，所有研究的植物都具有非共生血红蛋白，其生理作用尚不清楚。本研究探讨了三个代表性的类植物血红蛋白拟南芥：AtGLB1，AtGLB2和AtGLB3的催化功能。这些血红蛋白的纯化重组蛋白显示过氧化氢依赖性氧化的几种过氧化物酶底物，是敏感的氰化物，揭示内在的过氧化物酶样活性。在亚硝酸盐和过氧化氢的存在下，AtGLB1是最有效的介导酪氨酸硝化的自己和其他蛋白质通过形成活性氮物种作为亚硝酸盐氧化的结果。AtGLB1 mRNA在暴露于亚硝酸盐的拟南芥幼苗中显著积累，支持其功能与亚硝酸盐和亚硝酸盐衍生的活性氮物种的生理相关性。(C)2004年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.