蛋白质对细胞色素c中血红素的影响：来自拉曼差示光谱学的证据。
Protein influence on the heme in cytochrome c: evidence from Raman difference spectroscopy.
作者信息
Shelnutt J A, Rousseau D L, Dethmers J K, Margoliashi E
出版信息
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3865-9. doi: 10.1073/pnas.76.8.3865.
Abstract
Raman difference spectra have been obtained for the cytochromes c of a number of species by simultaneous data acquisition from two samples. Frequency differences as small as 0.1 cm-1 can be measured reproducibly by the technique we have developed. In comparisons between cytochromes c isolated from two different species, the frequency differences in the heme vibrational modes range from 0 to 6 cm-1. The vibrational frequencies of the heme are sensitive to the electronic charge density on the porphyrin macrocycle. The frequency differences are interpreted in terms of the influence of the heme-packed aromatic and highly electronegative amino acid side chains on the pi* charge density and distribution on the heme. Such a control of the electronic properties of the heme by the protein may be important for the function of cytochrome c.
摘要
通过同时采集两个样品的数据，获得了多个物种细胞色素c的拉曼差光谱。利用我们开发的技术，可以可重复地测量低至0.1 cm-1的频率差异。在比较从两个不同物种分离出的细胞色素c时，血红素振动模式的频率差异范围为0至6 cm-1。血红素的振动频率对卟啉大环上的电子电荷密度敏感。频率差异可以根据血红素周围堆积的芳香族和高电负性氨基酸侧链对血红素上π*电荷密度和分布的影响来解释。蛋白质对血红素电子性质的这种控制可能对细胞色素c的功能很重要。
相似文献
1
Protein influence on the heme in cytochrome c: evidence from Raman difference spectroscopy.蛋白质对细胞色素c中血红素的影响：来自拉曼差示光谱学的证据。
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3865-9. doi: 10.1073/pnas.76.8.3865.
2
Protein influences on porphyrin structure in cytochrome c: evidence from Raman difference spectroscopy.蛋白质对细胞色素c中卟啉结构的影响：拉曼差示光谱法提供的证据
Biochemistry. 1981 Oct 27;20(22):6485-97. doi: 10.1021/bi00525a030.
3
A comparative study of the resonance Raman spectra of bacterial cytochromes.细菌细胞色素的共振拉曼光谱的比较研究。
Arch Biochem Biophys. 1985 Feb 1;236(2):515-25. doi: 10.1016/0003-9861(85)90654-x.
4
Electronic and vibrational spectroscopy of the cytochrome c:cytochrome c oxidase complexes from bovine and Paracoccus denitrificans.牛和反硝化副球菌细胞色素c：细胞色素c氧化酶复合物的电子光谱和振动光谱
Protein Sci. 1992 Nov;1(11):1428-34. doi: 10.1002/pro.5560011104.
5
Resonance Raman scattering from hemoproteins. Effects of ligands upon the Raman spectra of various C-type cytochromes.血红蛋白的共振拉曼散射。配体对各种C型细胞色素拉曼光谱的影响。
J Biochem. 1975 Oct;78(4):719-28. doi: 10.1093/oxfordjournals.jbchem.a130960.
6
Resonance Raman spectroscopy of c-type cytochromes.
Biochimie. 1994;76(7):693-707. doi: 10.1016/0300-9084(94)90145-7.
7
Chromophore interactions in flavocytochrome c552: a resonance Raman investigation.黄素细胞色素c552中的发色团相互作用：共振拉曼光谱研究
Biochemistry. 1980 Apr 29;19(9):1723-30. doi: 10.1021/bi00550a001.
8
Resonance raman studies of a c type algal cytochrome. Deuterium shifts and a comparison with mammalian cytochrome c.一种c型藻类细胞色素的共振拉曼研究。氘位移及与哺乳动物细胞色素c的比较。
Biochim Biophys Acta. 1976 Jul 19;439(1):232-9. doi: 10.1016/0005-2795(76)90178-1.
9
Structural changes in cytochrome c upon hydrogen-deuterium exchange.细胞色素c在氢-氘交换后的结构变化。
Biochemistry. 1993 Dec 28;32(51):14158-64. doi: 10.1021/bi00214a013.
10
Investigations of the low frequency modes of ferric cytochrome c using vibrational coherence spectroscopy.利用振动相干光谱对铁细胞色素c的低频模式进行研究。
J Phys Chem B. 2014 Jun 12;118(23):6062-70. doi: 10.1021/jp501298c. Epub 2014 May 30.
引用本文的文献
1
Charge transfer stabilization of hemoglobin structures.血红蛋白结构的电荷转移稳定性
Biophys J. 1980 Oct;32(1):83-5. doi: 10.1016/S0006-3495(80)84920-4.
2
Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris.来自普通脱硫弧菌的2Fe-超氧化物还原酶中[Fe(His)(4)(Cys)]位点的光谱表征
J Biol Inorg Chem. 2003 Jul;8(6):671-82. doi: 10.1007/s00775-003-0465-4. Epub 2003 May 23.
3
Electron transfer in biological systems: an overview.生物系统中的电子转移：概述
Experientia. 1984 Jul 15;40(7):653-75. doi: 10.1007/BF01949719.
4
Heme-linked ionizations of myeloperoxidase detected by Raman difference spectroscopy. A comparison with plant and yeast peroxidases.通过拉曼差光谱检测髓过氧化物酶的血红素连接电离。与植物和酵母过氧化物酶的比较。
Biophys J. 1987 Apr;51(4):605-10. doi: 10.1016/S0006-3495(87)83385-4.
5
Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.血红蛋白中蛋白质与血红素的相互作用：拉曼差光谱法的证据
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4409-13. doi: 10.1073/pnas.76.9.4409.
本文引用的文献
1
Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution.高铁细胞色素c。I. 马和鲣鸟蛋白质在2.8埃分辨率下的一般特征。
J Biol Chem. 1971 Mar 10;246(5):1511-35.
2
Conformation of cytochromes c. IV. Conformational homology of functionally homologous cytochromes.细胞色素c的构象。IV. 功能同源细胞色素的构象同源性。
Biochim Biophys Acta. 1970 Jul 27;214(1):94-106.
3
Cytochrome c.细胞色素c
Adv Protein Chem. 1966;21:113-286. doi: 10.1016/s0065-3233(08)60128-x.
4
Resonance Raman spectra of hemoglobin and cytochrome c: inverse polarization and vibronic scattering.血红蛋白和细胞色素c的共振拉曼光谱：反偏振与振动散射
Proc Natl Acad Sci U S A. 1972 Sep;69(9):2622-6. doi: 10.1073/pnas.69.9.2622.
5
Resonance Raman spectra of heme proteins. Effects of oxidation and spin state.血红素蛋白的共振拉曼光谱。氧化和自旋态的影响。
J Am Chem Soc. 1974 Jan 23;96(2):338-45. doi: 10.1021/ja00809a004.
6
The mutational alteration of the primary structure of yeast iso-1-cytochrome c.酵母同工-1-细胞色素c一级结构的突变改变
J Biol Chem. 1968 Oct 25;243(20):5446-56.
7
An anomaly in the resonance Raman spectra of cytochrome P-450cam in the ferrous high-spin state.亚铁高自旋态的细胞色素P-450cam共振拉曼光谱中的异常现象。
J Biochem. 1976 Dec;80(6):1447-51. doi: 10.1093/oxfordjournals.jbchem.a131420.
8
Mitochondrial cytochrome c: preparation and activity of native and chemically modified cytochromes c.线粒体细胞色素c：天然及化学修饰细胞色素c的制备与活性
Methods Enzymol. 1978;53:128-64. doi: 10.1016/s0076-6879(78)53021-8.
9
Evolutionary change of the heme c electronic structure: ferricytochrome c-551 from Pseudomonas aeruginosa and horse heart ferricytochrome c.血红素c电子结构的进化变化：来自铜绿假单胞菌的高铁细胞色素c-551和马心高铁细胞色素c。
Biochem Biophys Res Commun. 1978 Aug 14;83(3):1132-9. doi: 10.1016/0006-291x(78)91513-9.
10
Structural homology of cytochromes c.
Eur J Biochem. 1978 Feb 1;83(1):261-75. doi: 10.1111/j.1432-1033.1978.tb12091.x.
Zotero 插件