Coupling crystallography and Computational biochemistry in understanding heme enzyme structure and function
Coupling crystallography and Computational biochemistry in understanding heme enzyme structure and function
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耦合晶体学和计算生物化学了解血红素酶的结构和功能
DOI：
10.1002/qua.10113
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发表时间：
2002
影响因子：
2.2
通讯作者：
Huiying Li
中科院分区：
文献类型：
--
作者：
T. Poulos;Tiffany P. Barrows;B. Bhaskar;C. A. Bonagura;Huiying Li
计算方法和晶体学已耦合到细胞色素c过氧化物酶（CCP）和一氧化氮合酶（NOS）的结构-功能关系的研究。NOS是一个重要的药物靶标，如果基于结构的药物设计在开发针对NOS的治疗剂中有任何用途，那么NOS-抑制剂相互作用的结构细节是必不可少的。7-硝基吲唑，一种有效的NOS抑制剂，复杂的一个NOS亚型的结构留下了一些模糊的抑制剂的精确定位。各种计算方法被用来解决这种模糊性，以及揭示紧密结合的能量基础。利用CCP定点诱变，结晶学和各种计算工具已被用于理解为什么CCP在催化期间稳定色氨酸阳离子自由基的能力在过氧化物酶中是独特的。© 2002 Wiley Periodicals，Inc.国际量子化学杂志，2002年
Computational methods and crystallography have been coupled to study structure–function relationships in cytochrome c peroxidase (CCP) and nitric oxide synthase (NOS). NOS is an important drug target and the structural details of NOS–inhibitor interactions are essential if structure-based drug design is to be of any use in the development of therapeutic agents targeted to NOS. The structure of 7-nitroindazole, a potent NOS inhibitor, complexed to one NOS isoform left some ambiguity in the precise orientation of the inhibitor. Various computational approaches were used to resolve this ambiguity as well as revealing the energetic basis for tight binding. With CCP site directed mutagenesis, crystallography and various computational tools have been used to understand why CCP is unique among the peroxidases in its ability to stabilize a tryptophan cation radical during catalysis. © 2002 Wiley Periodicals, Inc. Int J Quantum Chem, 2002
影响因子：
56.9
作者：
Crane, BR;Arvai, AS;Tainer, JA
通讯作者：
Tainer, JA