chromophore protonation state controls photoswitching of the fluoroprotein asfp595发色团质子化作用控制氟蛋白asfp595光电开关的状态.pdfVIP

Chromophore Protonation State Controls Photoswitching of the Fluoroprotein asFP595 ¨ 1 1 2 3 ¨ 1 Lars V. Schafer , Gerrit Groenhof , Martial Boggio-Pasqua , Michael A. Robb , Helmut Grubmuller * ¨ 1 Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Biophysical Chemistry, Gottingen, Germany, 2 Laboratoire de Chimie et Physique ´ Quantiques, IRSAMC, Universite Paul Sabatier, Toulouse, France, 3 Department of Chemistry, Imperial College London, London, United Kingdom Abstract Fluorescent proteins have been widely used as genetically encodable fusion tags for biological imaging. Recently, a new class of fluorescent proteins was discovered that can be reversibly light-switched between a fluorescent and a non- fluorescent state. Such proteins can not only provide nanoscale resolution in far-field fluorescence optical microscopy much below the diffraction limit, but also hold promise for other nanotechnological applications, such as optical data storage. To systematically exploit the potential of such photoswitchable proteins and to enable rational improvements to their properties requires a detailed understanding of the molecular switching mechanism, which is currently unknown. Here, we have studied the photoswitching mechanism of the reversibly switchable fluoroprotein asFP595 at the atomic level by multiconfigurational ab initio (CASSCF) calculations and QM/MM excited state molecular dynamics simulations with explicit surface hopping. Our simulations explain measured quantum yields and exc