发色团
蛋白质动力学
黄素组
化学
超短脉冲
光化学
黄蛋白
荧光
蛋白质结构
氨基酸
分子动力学
生物物理学
生物化学
物理
生物
计算化学
光学
激光器
酶
作者
Christopher R. Hall,Jinnette Tolentino Collado,James N. Iuliano,Agnieszka A. Gil,Katrin Adamczyk,András Lukács,Gregory M. Greetham,Igor V. Sazanovich,Peter J. Tonge,Stephen R. Meech
标识
DOI:10.1021/acs.jpcb.9b09425
摘要
Real-time observation of structure changes associated with protein function remains a major challenge. Ultrafast pump-probe methods record dynamics in light activated proteins, but the assignment of spectroscopic observables to specific structure changes can be difficult. The BLUF (blue light using flavin) domain proteins are an important class of light sensing flavoprotein. Here, we incorporate the unnatural amino acid (UAA) azidophenylalanine (AzPhe) at key positions in the H-bonding environment of the isoalloxazine chromophore of two BLUF domains, namely, PixD and AppABLUF; both proteins retain the red-shift on irradiation characteristic of photoactivity. Steady state and ultrafast time resolved infrared difference measurements of the azido mode reveal site-specific information on the nature and dynamics of light driven structure change. AzPhe dynamics are thus shown to be an effective probe of BLUF domain photoactivation, revealing significant differences between the two proteins and a differential response of the two sites to chromophore excitation.
科研通智能强力驱动
Strongly Powered by AbleSci AI