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Intermolecular Interactions and Intramolecular Couplings of Binuclear Porphyrin Models for Cytochrome c Oxidase.
Inorganic Chemistry ( IF 4.3 ) Pub Date : 2020-01-07 , DOI: 10.1021/acs.inorgchem.9b02958
Zhen Yao , Charles E Schulz 1 , Jiahui Yang 2 , Xiangjun Li , Jianfeng Li
Affiliation  

Cytochrome c oxidase (CcO) has a binuclear active site composed of a high-spin heme group and a tris-histidine-ligated copper ion (CuB). By using two different porphyrin models derived by Gunter (H2TPyPP) and us (H2TImPP), we have isolated several mono- and binuclear complexes including one carbonyl and three chloride derivatives which are determined by 100 K single-crystal X-ray. Low-temperature (4 K) EPR and multitemperature (295-25 K) Mössbauer investigations on the products not only confirmed the spin states of the two metal ions (S = 5/2 Fe3+ and S = 1/2 Cu2+) but also revealed the intermolecular interactions and intramolecular couplings which are in accordance with the crystal structural features.

中文翻译:

细胞色素c氧化酶的双核卟啉模型的分子间相互作用和分子内偶联。

细胞色素c氧化酶(CcO)具有双核活性位点,该位点由高纺血红素基团和三组氨酸连接的铜离子(CuB)组成。通过使用Gunter(H2TPyPP)和us(H2TImPP)衍生的两种不同的卟啉模型,我们分离了几种单核和双核配合物,其中包括一个羰基和三个氯化物衍生物,这些化合物通过100 K单晶X射线确定。低温(4 K)EPR和高温(295-25 K)的Mössbauer研究不仅证实了两种金属离子的自旋态(S = 5/2 Fe3 +和S = 1/2 Cu2 +),而且还揭示了根据晶体结构特征的分子间相互作用和分子内偶联。
更新日期:2020-01-07
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