Photoactive Yellow Protein, A New Type of Photoreceptor Protein: Will This “Yellow Lab” Bring Us Where We Want to Go?

作者：Klaas J. Hellingwerf, Johnny Hendriks, Thomas Gensch · 发表于：The Journal of Physical Chemistry A · 年份：2003 · DOI：10.1021/jp027005y · 被引用次数：285 · 研究领域：Photoreceptor and optogenetics research、Photosynthetic Processes and Mechanisms、bioluminescence and chemiluminescence research

Photoactive Yellow Protein ( PYP), discovered almost 20 years ago in Ectothiorhodospira (Halorhodospira) halophila, 1 is a 4-hydroxycinnamic acid-containing protein that functions as a blue-light photoreceptor in a behavioral avoidance response in this organism. During the past 10 years, PYP has become a model system for studies in photochemistry and protein folding, to the extent that it has become competitive with the rhodopsins. This is because PYP is small and very water-soluble, forms crystals readily (diffracting to high resolution), and shows excellent chemical- and photo-stability. These overall characteristics have allowed the application of an array of physicochemical techniques to analyze the biological function of PYP, i.e., the translation of a change of the configuration of its 4-hydroxycinnamic acid chromophore into an altered conformation of the surrounding protein. This has led to detailed insight into this process, both temporally and spatially, with respect to the structure of the transient intermediates involved, although we are still quite far from being able to track the position of all atoms in space, upon light activation of the protein in the relevant time domain. Nevertheless, the data already obtained may function as a calibration set in future work, to extend the time span of molecular dynamics simulations of conformational transitions in proteins to the time scale relevant for catalytic turnover. Occasionally, the application of multiple biophysic...