Regulation of cytochrome c oxidase activity by modulation of the catalytic site.
Regulation of cytochrome c oxidase activity by modulation of the catalytic site.
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DOI：
10.1038/s41598-018-29567-4
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发表时间：
2018-07-30
影响因子：
4.6
通讯作者：
Brzezinski P
中科院分区：
文献类型：
--
作者：
Schäfer J;Dawitz H;Ott M;Ädelroth P;Brzezinski P
酿酒酵母中的呼吸超复合物因子1（Rcf 1）与完整的细胞色素c氧化酶（CytcO）结合，并且也被认为是该酶的组装因子。在这里，我们使用亲和色谱法从rcf1Δ线粒体中分离CytcO，并研究还原、血红素间电子转移和配体与血红素a3的结合。数据显示去除Rcf1产生两个CytcO亚群。这些亚群之一表现出与从野生型菌株中分离的CytcO相同的功能行为，这表明完整的CytcO也在没有Rcf1的情况下组装。在另一个亚群中，先前显示出活性降低和配体结合动力学加速，催化位点的中点电位降低。较低的中点电位使我们能够选择性地减少rcf1Δ CytcO的两个亚群之一，这使得有可能分别研究两种CytcO形式的功能行为。我们推测，这些功能的改变反映了一种机制，调节O2的结合和捕获在CytcO，从而改变能量守恒的酶。
The respiratory supercomplex factor 1 (Rcf 1) in Saccharomyces cerevisiae binds to intact cytochrome c oxidase (CytcO) and has also been suggested to be an assembly factor of the enzyme. Here, we isolated CytcO from rcf1Δ mitochondria using affinity chromatography and investigated reduction, inter-heme electron transfer and ligand binding to heme a3. The data show that removal of Rcf1 yields two CytcO sub-populations. One of these sub-populations exhibits the same functional behavior as CytcO isolated from the wild-type strain, which indicates that intact CytcO is assembled also without Rcf1. In the other sub-population, which was shown previously to display decreased activity and accelerated ligand-binding kinetics, the midpoint potential of the catalytic site was lowered. The lower midpoint potential allowed us to selectively reduce one of the two sub-populations of the rcf1Δ CytcO, which made it possible to investigate the functional behavior of the two CytcO forms separately. We speculate that these functional alterations reflect a mechanism that regulates O2 binding and trapping in CytcO, thereby altering energy conservation by the enzyme.
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影响因子：
4.8
作者：
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通讯作者：
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发表时间：
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影响因子：
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通讯作者：
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