Structural studies on Desulfovibrio gigas cytochrome c3 by two-dimensional 1H-nuclear-magnetic-resonance spectroscopy.
Structural studies on Desulfovibrio gigas cytochrome c3 by two-dimensional 1H-nuclear-magnetic-resonance spectroscopy.
复制标题
通过二维 1H 核磁共振波谱对脱硫弧菌细胞色素 c3 进行结构研究。
DOI：
10.1042/bj2940909
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Xavier,AV
中科院分区：
文献类型：
--
作者：
Piçarra-Pereira,MA;Turner,DL;LeGall,J;Xavier,AV
基于芳香族氨基酸的质子与血红素质子之间的相互作用以及x射线结构中已知的血红素距离，使用二维1H nmr对完全还原形式的Desulfovibrio gigas cytochrome c3中的几个芳香氨基酸残基和血红素共振进行了分配[Kissinger (1989) Ph.D. Thesis, Washington State University]。在新核磁共振光谱中观察到的间质相互作用与D. gigas x射线结构完全一致，也与来自Desulfovibrio vulgaris （Hildenborough）的新核磁共振数据一致[Turner， Salgueiro， LeGall和Xavier(1992)]。[j].中国生物医学工程学报，2016,33(2):391 - 391。计算出的环电流位移与观测到的化学位移之间的良好相关性有力地支持了目前的分配。通过观察蛋白质在还原、中间和完全氧化阶段的二维核-奥弗豪斯增强光谱，可以根据其中点氧化还原电位和x射线结构对其进行排序。第一个被氧化的血红素是血红素I，其次是血红素II、III和IV，根据氨基酸序列中的Cys配体位置编号[Mathews (1985) Prog。Biophys。生物化学学报，2004,18(2):444 - 444。虽然不同的Desulfovibrio细胞色素c3的血红素核心结构相同，但氧化还原电位的顺序不同。
Several aromatic amino acid residues and haem resonances in the fully reduced form of Desulfovibrio gigas cytochrome c3 are assigned, using two-dimensional 1H n.m.r., on the basis of the interactions between the protons of the aromatic amino acids and the haem protons as well as the intrahaem distances known from the X-ray structure [Kissinger (1989) Ph.D. Thesis, Washington State University]. The interhaem interactions observed in the n.m.r. spectra are in full agreement with the D. gigas X-ray structure and also with the n.m.r. data from Desulfovibrio vulgaris (Hildenborough) [Turner, Salgueiro, LeGall and Xavier (1992) Eur. J. Biochem. 210, 931-936]. The good correlation between the calculated ring-current shifts and the observed chemical shifts strongly supports the present assignments. Observation of the two-dimensional nuclear-Overhauser-enhancement spectra of the protein in the reduced, intermediate and fully oxidized stages led to the ordering of the haems in terms of their midpoint redox potentials and their identification in the X-ray structure. The first haem to oxidize is haem I, followed by haems II, III and IV, numbered according to the Cys ligand positions in the amino acid sequences [Mathews (1985) Prog. Biophys. Mol. Biol. 54, 1-56]. Although the haem core architecture is the same for the different Desulfovibrio cytochromes c3, the order of redox potentials is different.