Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles.
Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles.
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DOI：
10.1021/la052035o
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发表时间：
2005-12
期刊：
影响因子：
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通讯作者：
Renjis T. Tom;T. Pradeep
中科院分区：
文献类型：
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作者：
Renjis T. Tom;T. Pradeep
本文研究了代谢抑制剂叠氮与固定在Au和Ag纳米颗粒上的氯化高铁血红素(Hem)和细胞色素c(Cytc)的结合作用。各种光谱工具已经被用来了解纳米颗粒表面发生的化学作用。通过紫外-可见光谱、荧光光谱、傅里叶变换红外光谱和拉曼光谱研究了模型体系氯化血红素的结合性质，并用MALDI-TOF MS详细研究了叠氮结合的机理。用质谱仪检测到了纳米颗粒表面的氯化高铁血红素-N(3)加合物，并对其碎片进行了源后衰变分析。将氯化血红素在纳米颗粒表面的化学与蛋白质Cytc进行了比较。与氯化高铁血红素不同，Cytc的叠氮化物结合需要热激活，因为血红素中心的可及性降低。与纳米颗粒结合的游离细胞色素c和细胞色素c的结合化学相似。
This paper presents a set of investigations on the binding of a metabolic inhibitor, azide with prosthetic heme group of biomolecules, hemin chloride (Hem) and cytochrome c (Cyt c) immobilized on Au and Ag nanoparticles. A variety of spectroscopic tools have been used to understand the chemistry occurring on the nanoparticle surface. While the nature of binding of the model system, hemin has been investigated by UV-visible, fluorescence, FTIR, and Raman spectroscopies, the azide binding has been studied in detail by MALDI-TOF MS. Hemin binding on the nanoparticle surface occurs through the carboxylic acid groups. The hemin-N(3) adduct on the nanoparticle surface has been detected by mass spectrometry and its fragments have been studied by post source decay analysis. The chemistry of hemin on the nanoparticle surface has been compared with that of the protein, Cyt c. Azide binding of Cyt c requires thermal activation due to reduced accessibility of the heme center, unlike in the case of hemin. The binding chemistry is similar for free Cyt c and Cyt c bound to the nanoparticles.