Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy.
Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy.
复制标题
通过共振拉曼光谱对酵母 iso-1 细胞色素 c 突变体进行结构研究。
DOI：
10.1111/j.1432-1033.1991.tb16276.x
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
R. J. Williams
中科院分区：
文献类型：
--
作者：
P. Hildebrandt;G. Pielak;R. J. Williams
用共振拉曼光谱法研究了酵母iso-1细胞色素c的Ser 82和Phe 82变体。在这两种氧化态下，观察到明显的光谱变化的一些频带中的低频区域，这敏感地响应于构象扰动的血红素的蛋白质环境。这些谱带可归属于包括主要局限于携带丙酸酯的吡咯环A和D中的振动的强贡献的模式。这表明在血红素裂隙的较深部分的结构差异，远离突变位点。这一结论与以前的X射线晶体学和NMR光谱学的结果一致。共振拉曼光谱中没有观察到差异，这可以直接与突变位点附近的血红素口袋的构象变化。温度依赖性的共振拉曼实验的氧化突变体显示光谱的变化，这是密切相关的细胞色素c吸附后，带电的银表面的表面增强共振拉曼光谱。这些光谱变化可归因于血红素裂隙的开放伴随着铁-甲硫氨酸配体键的弱化。温度依赖性构象转变发生在约30摄氏度的Ser 82变体和在约45摄氏度的Phe 82变体，这意味着Phe-Ser取代显着降低血红素口袋的热稳定性。两种突变体的还原形式在高达65 ℃下是稳定的。
The Ser82 and Phe82 variants of yeast iso-1 cytochrome c were studied by resonance Raman spectroscopy. In both oxidation states, distinct spectral changes were observed for some of those bands in the low-frequency region, which sensitively respond to conformational perturbations of the protein environment of the heme. These bands can be assigned to modes which include strong contributions of vibrations largely localized in the propionate-carrying pyrrole rings A and D. This indicates structural differences in the deeper part of the heme crevice, remote from the mutation site. This conclusion is in line with previous results from X-ray crystallography and NMR spectroscopy. No differences in the resonance-Raman spectra were observed which can be directly correlated with conformational changes of the heme pocket in the vicinity of the mutation site. Temperature-dependent resonance Raman experiments of the oxidized mutants revealed spectral changes which are closely related to those observed for cytochrome c upon adsorption to charged silver surfaces by surface-enhanced resonance Raman spectroscopy. These spectral changes can be attributed to an opening of the heme crevice accompanied by a weakening of the iron-methionine ligand bond. The temperature-dependent conformational transition occurs at approximately 30 degrees C for the Ser82 variant and at about 45 degrees C for the Phe82 variant, implying that the Phe----Ser substitution significantly lowers the thermal stability of the heme pocket. The reduced forms of both mutants are stable up to 65 degrees C.
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87 位具有苯丙氨酸或酪氨酸的酵母细胞色素 c 将电子转移至（锌细胞色素 c 过氧化物酶），其速度是丝氨酸 87 或甘氨酸 87 变体的一万倍。
DOI：
10.1073/pnas.84.5.1249
发表时间：
1987
影响因子：
11.1
作者：
Liang,N;Pielak,GJ;Mauk,AG;Smith,M;Hoffman,BM
通讯作者：
Hoffman,BM
细胞色素c过氧化物酶的假设模型。
DOI：
--
发表时间：
1980
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Poulos,TL;Kraut,J
通讯作者：
Kraut,J
复合物形成时细胞色素 c 和细胞色素氧化酶的构象变化：共振拉曼研究。
影响因子：
2.9
作者：
Hildebrandt,P;Heimburg,T;Marsh,D;Powell,GL
通讯作者：
Powell,GL
苯丙氨酸 82 在酵母 iso-1-细胞色素 c 中的作用以及该位置丝氨酸残基诱导的远程构象变化。
影响因子：
2.9
作者：
Louie,GV;Pielak,GJ;Smith,M;Brayer,GD
通讯作者：
Brayer,GD
突变诱导的细胞色素 c 碱性转变的扰动。
影响因子：
2.9
作者：
Pearce,LL;Gärtner,AL;Smith,M;Mauk,AG
通讯作者：
Mauk,AG