Ritter, E.; Puskar, L.; Kim, S.Y.; Park, J.H.; Hofmann, K.P.; Bartl, F.; Hegemann, P.; Schade, U.: Féry Infrared Spectrometer for Single-Shot Analysis of Protein Dynamics. Journal of Physical Chemistry Letters 10 (2019), p. 7672-7677

Current submillisecond time-resolved broad-band infrared spectrosco-py, one of the most frequently used techniques for studying structure−functionrelationships in life sciences, is typically limited to fast-cycling reactions that can berepeated thousands of times with high frequency. Notably, a majority of chemical andbiological processes do not comply with this requirement. For example, the activationof vertebrate rhodopsin, a prototype of many protein receptors in biological organismsthat mediate basic functions of life, including vision, smell, and taste, is irreversible.Here we present a dispersive single-shot Féry spectrometer setup that extends suchspectroscopy to irreversible and slow-cycling systems by exploiting the uniqueproperties of brilliant synchrotron infrared light combined with an advanced focalplane detector array embedded in a dispersive optical concept. We demonstrate oursingle-shot method on microbial actinorhodopsin with a slow photocycle and onvertebrate rhodopsin with irreversible activation.