15N标记的古菌型铁硫蛋白的二维脉冲电子自旋共振表征
Two-dimensional pulsed electron spin resonance characterization of 15N-labeled archaeal Rieske-type ferredoxin.
作者信息
Iwasaki Toshio, Samoilova Rimma I, Kounosu Asako, Dikanov Sergei A
机构信息
Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Tokyo 113-8602, Japan.
出版信息
FEBS Lett. 2009 Nov 3;583(21):3467-72. doi: 10.1016/j.febslet.2009.09.050. Epub 2009 Oct 3.
Abstract
Two-dimensional electron spin-echo envelope modulation (ESEEM) analysis of the uniformly (15)N-labeled archaeal Rieske-type [2Fe-2S] ferredoxin (ARF) from Sulfolobus solfataricus P1 has been conducted in comparison with the previously characterized high-potential protein homologs. Major differences among these proteins were found in the hyperfine sublevel correlation (HYSCORE) lineshapes and intensities of the signals in the (++) quadrant, which are contributed from weakly coupled (non-coordinated) peptide nitrogens near the reduced clusters. They are less pronounced in the HYSCORE spectra of ARF than those of the high-potential protein homologs, and may account for the tuning of Rieske-type clusters in various redox systems.
摘要
对来自嗜热栖热菌P1的均匀（15）N标记的古菌型里斯克型[2Fe-2S]铁氧化还原蛋白（ARF）进行了二维电子自旋回波包络调制（ESEEM）分析，并与先前表征的高电位蛋白同源物进行了比较。这些蛋白质之间的主要差异在于超精细子能级相关（HYSCORE）线形以及（++）象限中信号的强度，这些差异来自还原簇附近弱耦合（非配位）的肽氮。与高电位蛋白同源物相比，ARF的HYSCORE光谱中这些差异不太明显，这可能解释了各种氧化还原系统中里斯克型簇的调节情况。
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