Probing membrane enhanced protein-protein interactions in a minimal redox complex of cytochrome-P450 and P450-reductase
Probing membrane enhanced protein-protein interactions in a minimal redox complex of cytochrome-P450 and P450-reductase
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DOI：
10.1039/c9cc01630a
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发表时间：
2019-05-21
影响因子：
4.9
通讯作者：
Ramamoorthy, Ayyalusamy
中科院分区：
文献类型：
--
作者：
Mahajan, Mukesh;Ravula, Thirupathi;Ramamoorthy, Ayyalusamy
研究细胞色素-P450及其还原酶的最小氧化还原复合物中的相互作用对于理解细胞色素-P450的酶活性至关重要。使用NMR探测动态结构相互作用的热点揭示了来自P450-还原酶的环残基的参与，负责CYP 450对其专性氧化还原伴侣的亲和力增强。
Investigating the interplay in a minimal redox complex of cytochrome-P450 and its reductase is crucial for understanding cytochrome-P450' s enzymatic activity. Probing the hotspots of dynamic structural interactions using NMR revealed the engagement of loop residues from P450-reductase to be responsible for the enhanced affinity of CYP450 towards its obligate redox partner.