ESEEM studies of succinate:ubiquinone reductase from Paracoccus denitrificans.
ESEEM studies of succinate:ubiquinone reductase from Paracoccus denitrificans.
复制标题
来自脱氮副球菌的琥珀酸：泛醌还原酶的 ESEEM 研究。
DOI：
10.1007/s007750000142
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Chan,SI
中科院分区：
文献类型：
--
作者：
Hung,SC;Grant,CV;Peloquin,JM;Waldeck,AR;Brit,RD;Chan,SI
利用电子自旋回波包络调制（ESEEM）光谱技术，对副球菌琥珀酸泛醌还原酶中还原态[2Fe-2S]簇（S-1中心）、氧化态[3Fe-4S]簇（S-3中心）和黄素半醌自由基的环境进行了研究.从还原[2Fe-2S]的ESEEM数据的光谱模拟产生了指示肽氮的核四极相互作用参数。我们还观察到氧化的[3Fe-4S]簇和肽14 N之间的弱相互作用。没有证据表明任何Fe原子与咪唑环的14 N原子配位。黄素半醌自由基的ESEEM数据较为复杂。在这里，未成对电子和黄素环中的两个氮原子之间的相互作用得到了证据。
Electron spin-echo envelope modulation (ESEEM) spectroscopy has been performed in order to obtain structural information about the environment of the reduced [2Fe-2S] cluster (S-1 center), the oxidized [3Fe-4S] cluster (S-3 center), and the flavin semiquinone radical in purified succinate:ubiquinone reductase fromParacoccus denitrificans. Spectral simulations of the ESEEM data from the reduced [2Fe-2S] yielded nuclear quadrupole interaction parameters that are indicative of peptide nitrogens. We also observed a weak interaction between the oxidized [3Fe-4S] cluster and a peptide14N. There was no evidence for coordination of any of the Fe atoms to14N atoms of imidazole rings. The ESEEM data from the flavin semiquinone radical were more complicated. Here, evidence was obtained for interactions between the unpaired electron and only the two nitrogen atoms in the flavin ring.