Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: binding of ligands at the arginine site induces changes in the heme ligation geometry.
Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: binding of ligands at the arginine site induces changes in the heme ligation geometry.
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诱导型一氧化氮合酶血红素结构域的电子顺磁共振波谱：配体在精氨酸位点的结合诱导血红素连接几何结构的变化。
DOI：
10.1021/bi960607l
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Masters,BS
中科院分区：
文献类型：
--
作者：
Salerno,JC;Martasek,P;Roman,LJ;Masters,BS
诱导型一氧化氮合酶 (iNOS) 血红素结构域的电子顺磁共振谱表明与神经元亚型 (nNOS) 的相应谱有密切关系。配体与 iNOS 精氨酸位点的结合以高度配体特异性的方式扰乱高自旋铁血红素的环境。 iNOS 与精氨酸类似物形成五配位、高自旋复合物，该复合物与相应的 nNOS 复合物明显相关。研究表明，l-精氨酸、Nω-羟基-l-精氨酸 (NHA) 和 Nω-甲基-l-精氨酸 (NMA) 的结合产生与 nNOS 等价复合物密切对应的各种光谱物质，而 Nω-硝基-l-精氨酸 (NNA) 结合产生介于 nNOS NNA 和精氨酸复合物之间的中间状态。这些光谱研究可以确定配体特异性的高自旋态，揭示 iNOS 和 nNOS 之间的异同。
The electron paramagnetic resonance spectra of the heme domain of inducible nitric oxide synthase (iNOS) demonstrate a close relationship to the corresponding spectra of the neuronal isoform (nNOS). The binding of ligands to the iNOS arginine site perturbs the environment of the high-spin ferriheme in a highly ligand-specific manner. The iNOS forms five-coordinate, high-spin complexes with arginine analogs which are clearly related to the corresponding complexes of nNOS. Studies indicate that the binding ofl-arginine,Nω-hydroxy-l-arginine (NHA), andNω-methyl-l-arginine (NMA) produces various spectroscopic species closely corresponding to the equivalent complexes of nNOS, whileNω-nitro-l-arginine (NNA) binding produces a state which appears intermediate in character between the nNOS NNA and arginine complexes. These spectroscopic studies have permitted the determination of ligand-specific high-spin states which reveal similarities and differences between iNOS and nNOS.