Isolation and characterization of vibrational spectra of individual heme active sites in cytochrome bc1 complexes from Rhodobacter capsulatus.
Isolation and characterization of vibrational spectra of individual heme active sites in cytochrome bc1 complexes from Rhodobacter capsulatus.
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荚膜红杆菌细胞色素 bc1 复合物中单个血红素活性位点振动光谱的分离和表征。
DOI：
10.1021/bi960419v
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发表时间：
1996
期刊：
影响因子：
2.9
通讯作者：
Ondrias,MR
中科院分区：
文献类型：
--
作者：
Gao,F;Qin,H;Simpson,MC;Shelnutt,JA;Knaff,DB;Ondrias,MR
用不同激发波长获得了荚膜红细菌（Rhodobacter capsulatus）bc 1复合物和分离的c1亚基的共振拉曼光谱。通过Q-带激发的bc 1复合物在不同的氧化还原状态下获得的光谱被分离，以产生个人的三个血红素活性位点的振动光谱。HemesbHandc 1分别具有b型和c型血红素的典型振动光谱。与此相反，hemebL的光谱相对于其他hemesb是异常的。孤立的光谱也被用来评估抑制剂结合的血红素的局部结构环境的影响。无论是抗霉素，也不myxothiazol结合产生戏剧性的结构扰动的血红素。Hemec 1完全不受任一抑制剂的影响。hemesbHandbL的振动光谱分别被抗霉素和粘噻唑结合而轻微改变。
Resonance Raman spectra ofbc1complexes and isolatedc1subunit fromRhodobacter capsulatushave been obtained using a variety of excitation wavelengths. Spectra obtained via Q-band excitation ofbc1complexes in different redox states were separated to yield the individual vibrational spectra of each of the three heme active sites. HemesbHandc1exhibit vibrational spectra typical ofb- andc-type hemes, respectively. In contrast, the spectrum of hemebLis anomalous with respect to those of other hemesb. The isolated spectra were also used to assess the effects of inhibitor binding on the local structural environments of the hemes. Neither antimycin nor myxothiazol binding produces dramatic structural perturbations at the hemes. Hemec1is completely unaffected by the presence of either inhibitor. The vibrational spectra of hemesbHandbLare slightly altered by antimycin and myxothiazol binding, respectively.