TIME RESOLVED TRYPTOPHAN FLUORESCENCE FROM CYTOCHROME B5

分子动力学模拟揭示了暴露的血红素边缘， 在细胞色素的任何晶体或核磁共振结构中均未观察到 B5. 这一裂缝可能具有重要的功能， 介导直接电子转移的氧化还原配偶体的识别 对于一些复杂的。 为了研究裂隙呼吸的动力学 我们开始了单一Trp-22的稳态荧光研究。 丙烯酰胺淬灭单个色氨酸大鼠细胞色素b5和 它的各种二硫化物突变体进行了检查， 谱 为了探索假定裂缝的动力学， 另外的色氨酸已被置于表面上（S18 W）。 野生型的寿命分布和各向异性衰变的比较 Trp-18突变体可能提供了关于细胞迁移率的新信息。 蛋白质表面的裂缝区域。

Molecular dynamic simulations reveal an exposed heme edge that has not been observed in any crystal or NMR structure of cytochrome b5. This cleft is likely to be of functional importance for recognition of a redox partner for mediating direct electron transfer for some complexes. In order to study dynamics of the cleft breathing we initiated a steady-state fluorescence study of single Trp-22. Acrylamide quenching of the single tryptophan rat cytochrome b5 and its various disufide mutants was examined by ultrafast time-resolved spectroscopy. In order to probe dynamics of the putative cleft, an additional tryptophan has been placed on the surface (S18W). Comparison of lifetime distribution and anisotropy decays of wild-type and mutant with Trp-18 may provide new information about mobility of the protein surface in the cleft region of the protein.