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首页> 美国政府科技报告 >Analyzing Xanthine Dehydrogenase Iron-Sulfur Clusters Using Electron Paramagnetic Spectroscopy
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Analyzing Xanthine Dehydrogenase Iron-Sulfur Clusters Using Electron Paramagnetic Spectroscopy

机译：用电子顺磁光谱分析黄嘌呤脱氢酶铁硫簇

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Xanthine dehydrogenase is a metalloenzyme that is present in a variety of eukaryotic and prokaryotic organisms. The oxidation of the xanthine occurs at the molybdenum site, and the catalytic cycle is completed by electron transfer to the iron-sulfur (Fe/S) clusters and finally the flavin, where they are accepted by nicotinamide adenine dinucleotide (NAD). Since the site giving rise to the Fe/S I electron paramagnetic resonance (EPR) signal is thought to be the initial recipient of the electrons from the Mo, we wish to understand which EPR signal is associated with which Fe/S cluster in the structure in order to develop an understanding of the electron flow within the molecule. Samples of xanthine dehydrogenase wild-type and mutant forms were analyzed with EPR spectroscopy techniques at low and high temperatures. The results showed an altered Fe/S I signal along with an unaltered Fe/S 11 signal.

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