A theoretical study on the binding of O2, NO and CO to heme proteins
A theoretical study on the binding of O2, NO and CO to heme proteins
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DOI：
10.1016/j.jinorgbio.2005.02.014
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发表时间：
2005-04-01
影响因子：
3.9
通讯作者：
Siegbahn, PEM
中科院分区：
文献类型：
--
作者：
Blomberg, LM;Blomberg, MRA;Siegbahn, PEM
采用杂化密度泛函B3 LYP方法研究了O-2、NO和CO等双原子分子与亚铁血红素的成键过程。三种不同的模型，一个五配位的卟啉在苯中，肌红蛋白的活性位点，包括远端组氨酸和双核中心的细胞色素氧化酶。B3 LYP泛函很好地描述了几何和电子结构，而实验结合能更难再现。发现细胞色素氧化酶中的CUB中心与肌红蛋白中的末端组氨酸对蛋白质的结合有类似的作用。(c)2005年爱思唯尔公司All rights reserved.
The hybrid density functional B3LYP is used to describe the bonding of the diatomic molecules O-2, NO and CO to ferrous heme. Three different models are used, a five-coordinated porphyrin in benzene, the myoglobin active site including the distal histidine and the binuclear center in cytochrome oxidase. The geometric and electronic structures are well described by the B3LYP functional, while experimental binding energies are more difficult to reproduce. It is found that the CUB center in cytochrome oxidase has a similar effect on the binding of the diatomics as the distal histidine in myoglobin. (c) 2005 Elsevier Inc. All rights reserved.