EXCITED STATE OF HEME & EFFECTS ON PROTEIN STRUCT BY EXCITATION ENERGY TRANSFER

我们测量了马的时间分辨发射强度衰变 心脏肌红蛋白和四聚体人血红蛋白在两次脉搏下的变化 激励条件。第一个脉冲580 nm激发血红素(For CO形成光解离配体)并诱导构象 血球蛋白结构改变。第二个脉冲290 nm激发 色氨酸在设定的延迟后。色氨酸寿命分布 在给定的秒脉冲延迟下测量，即使对很小的 色氨酸和血红素之间的距离变化。通过应用Forster 色氨酸间无辐射激发能量转移模型 和血红素我们可以解释和跟踪蛋白质构象的变化 从皮秒到毫秒的时间范围。这些研究只是 可能是因为关于光淬火的核心技术项目 CFS。

We measured the time-resolved emission intensity decay of horse heart myoglobin and tetrameric human hemoglobin under two pulse excitation conditions. The first pulse 580 nm excites the heme (for CO form photodissociate the ligand) and induces a conformational change of hemoprotein structure. The second pulse 290 nm excites tryptophan after a set delay. The tryptophan lifetime distribution measured at given second pulse delay is very sensitive to even small distance changes between tryptophan and heme. By applying the Forster model of radiationless excitation energy transfer between tryptophan and heme we can interpret and follow protein conformational changes from picosecond to a millisecond time range. These studies are only possible because of the core technology project on light quenching at the CFS.