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减 双脉冲下心肌红蛋白和四聚体人血红蛋白 激发条件 第一脉冲580 nm激发血红素（对于 CO形式光解离配体）并诱导构象 血红素蛋白结构改变。 第二脉冲290 nm激发 在设定的延迟之后的色氨酸。 色氨酸寿命分布 在给定的第二脉冲延迟下测量的脉冲宽度对即使很小的 色氨酸和血红素之间的距离变化。 通过应用福斯特 色氨酸与色氨酸之间的无辐射激发能转移模型 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 由于光猝灭的核心技术项目， 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.