Probing the oxygen activation reaction in intact whole mitochondria through analysis of molecular vibrations.
Probing the oxygen activation reaction in intact whole mitochondria through analysis of molecular vibrations.
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DOI：
10.1021/ja051761a
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发表时间：
2005-07
影响因子：
15
通讯作者：
Toshinari Takahashi;S. Kuroiwa;T. Ogura;S. Yoshikawa
中科院分区：
文献类型：
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作者：
Toshinari Takahashi;S. Kuroiwa;T. Ogura;S. Yoshikawa
利用一种新型的时间分辨共振拉曼测量系统检测完整的猪线粒体样品，研究了细胞色素C氧化酶催化的氧还原过程，其实验准确度相当于溶解和纯化的酶反应体系的准确度。可分配给最初三个中间体的共振拉曼谱带的频率与纯化酶制剂的频率相同。然而，线粒体制剂中的初始中间体(含氧物种)的寿命明显长于纯化制剂中的观察到的寿命，这表明线粒体制剂中含氧物种的稳定性是由线粒体膜系统施加控制的。
The process of dioxygen reduction catalyzed by cytochrome c oxidase was investigated by examining intact porcine mitochondrial preparations using a novel time-resolved resonance Raman measurement system at experimental accuracy levels equivalent to those of the reaction system of the solubilized and purified enzyme. The resonance Raman bands assignable to the initial three intermediates were detected at frequencies identical to those observed with purified enzyme preparations. However, the lifetime of the initial intermediate (the oxygenated species) in the mitochondrial preparation was found to be significantly longer than that observed in purified preparations, suggesting that control of the stability of the oxygenated species is imposed by the mitochondrial membrane system.