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Front Cover: Electrochemical Activity of Cytochrome P450 1A2: The Relevance of O2 Control and the Natural Electron Donor (ChemElectroChem 3/2021)
ChemElectroChem ( IF 4 ) Pub Date : 2021-01-14 , DOI: 10.1002/celc.202001616
Célia M. Silveira 1, 2 , Patrícia R. Rodrigues 1, 3 , Wissam Ghach 4 , Sofia A. Pereira 5 , Francisco Esteves 6 , Michel Kranendonk 6 , Mathieu Etienne 4 , M. Gabriela Almeida 1, 7
Affiliation  

The Front Cover shows the electrochemical response of the human monooxygenase enzyme, cytochrome P450 1A2 (CYP1A2), in the presence of its natural electron donor partner, cytochrome P450 oxidoreductase (CPR), highlighting the role of the interaction with the latter in the stabilization of CYP1A2 and attaining the electrochemically driven activity towards O2. The picture also emphasizes the protein entrapment matrix, a biocompatible sol‐gel film, which proved to be crucial for the achievement of interfacial electron transfer. More information can be found in the Article by M. G. Almeida and co‐workers.
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中文翻译:

封面:细胞色素P450 1A2的电化学活性:氧气控制与天然电子给体的相关性(ChemElectroChem 3/2021)

前盖显示了在自然电子供体伴侣细胞色素P450氧化还原酶(CPR)存在的情况下人单加氧酶酶细胞色素P450 1A2(CYP1A2)的电化学响应,突出了与后者的相互作用在稳定细胞色素P450 1A2中的作用。 CYP1A2并获得对O 2的电化学驱动活性。图片还强调了蛋白质捕获基质(一种生物相容的溶胶-凝胶薄膜),它被证明对实现界面电子转移至关重要。有关更多信息,请参见M. G. Almeida及其同事的文章。
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更新日期:2021-02-01
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