Cartling B
Biophys J. 1983 Aug;43(2):191-205. doi: 10.1016/S0006-3495(83)84340-9.
Stabilized intermediate redox states of cytochrome c are generated by radiolytic reduction of initially oxidized enzyme in glass matrices at liquid nitrogen temperature. In the intermediate states the heme group is reduced by hydrated electrons, whereas the protein conformation is restrained close to its oxidized form by the low-temperature glass matrix. The intermediate and stable redox states of cytochrome c at neutral and alkaline pH are studied by low-temperature resonance Raman spectroscopy using excitations in resonance with the B (Soret) and Q1 (beta) optical transitions. The assignments of the cytochrome c resonance Raman bands are discussed. The observed spectral characteristics of the intermediate states as well as of the alkaline transition in the oxidized state are interpreted in terms of oxidation-state marker modes, spin-state marker modes, heme iron--axial ligand stretching modes, totally symmetric in-plane porphyrin modes, nontotally symmetric in-plane modes, and out-of-plane modes.
在液氮温度下,通过玻璃基质中初始氧化酶的辐射还原作用,可生成细胞色素c的稳定中间氧化还原态。在中间态,血红素基团被水合电子还原,而蛋白质构象则因低温玻璃基质而被限制在接近其氧化形式的状态。利用与B(索雷特)和Q1(β)光学跃迁共振的激发,通过低温共振拉曼光谱研究了中性和碱性pH条件下细胞色素c的中间态和稳定氧化还原态。讨论了细胞色素c共振拉曼谱带的归属。根据氧化态标记模式、自旋态标记模式、血红素铁 - 轴向配体伸缩模式、完全对称的面内卟啉模式、非完全对称的面内模式和面外模式,对中间态以及氧化态碱性转变的观察光谱特征进行了解释。