Department of Physics and Chemistry, University of Palermo , Viale delle Scienze, 90128 Palermo, Italy.
LCLS, SLAC National Accelerator Laboratory , Menlo Park, California 94025, USA.
Struct Dyn. 2015 May 29;2(4):041713. doi: 10.1063/1.4921907. eCollection 2015 Jul.
We report time-resolved X-ray absorption measurements after photolysis of carbonmonoxy myoglobin performed at the LCLS X-ray free electron laser with nearly 100 fs (FWHM) time resolution. Data at the Fe K-edge reveal that the photoinduced structural changes at the heme occur in two steps, with a faster (∼70 fs) relaxation preceding a slower (∼400 fs) one. We tentatively attribute the first relaxation to a structural rearrangement induced by photolysis involving essentially only the heme chromophore and the second relaxation to a residual Fe motion out of the heme plane that is coupled to the displacement of myoglobin F-helix.
我们在 LCLS 自由电子激光上进行了一氧化碳肌红蛋白光解的时间分辨 X 射线吸收测量,时间分辨率接近 100fs(半峰全宽)。在铁 K 边的数据表明,在卟啉环处的光诱导结构变化分两步发生,较快的(约 70fs)弛豫先于较慢的(约 400fs)弛豫。我们初步将第一个弛豫归因于光解诱导的结构重排,该重排基本上只涉及卟啉环发色团,第二个弛豫归因于残留在卟啉环外的铁原子的运动,该运动与肌红蛋白 F 螺旋的位移相关。