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Journal Article

Time-Resolved Energetics of Photoprocesses in Prokaryotic Phytochrome-Related Photoreceptors

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Citation

Losi, A., Bonomi, H. R., Michael, N., Tang, K., & Zhao, K.-H. (2017). Time-Resolved Energetics of Photoprocesses in Prokaryotic Phytochrome-Related Photoreceptors. Photochemistry and Photobiology, 93(3), 733-740. doi:10.1111/php.12728.


Cite as: http://hdl.handle.net/21.11116/0000-0007-1893-8
Abstract
Time-resolved photoacoustics (PA) is uniquely able to explore the energy landscape of photoactive proteins and concomitantly detects light-induced volumetric changes (V) accompanying the formation and decay of transient species in a time window between ca. 20ns and 5 mu s. Here, we report PA measurements on diverse photochromic bilin-binding photoreceptors of prokaryotic origin: (1) the chromophore-binding GAF3 domain of the red (R)/green (G) switching cyanobacteriochrome 1393 (Slr1393g3) from Synechocystis; (2) the red/far red (R/FR) Synechocystis Cph1 phytochrome; (3) full-length and truncated constructs of Xanthomonas campestris bacteriophytochrome (XccBphP), absorbing up to the NIR spectral region. In almost all cases, photoisomerization results in a large fraction of energy dissipated as heat (up to 90%) on the sub-ns scale, reflecting the low photoisomerization quantum yield (<0.2). This prompt step is accompanied by a positive Delta V-1=5-12.5 mL mol(-1). Formation of the first intermediate is the sole process accessible to PA, with the notable exception of Slr1393g3-G for which Delta V-1= +4.5mLmol(-1) is followed by a time-resolved, energy-conserving contraction Delta V-2=-11.4 mL mol(-1), tau(2)=180 ns at 2.4 degrees C. This peculiarity is possibly due to a larger solvent occupancy of the chromophore cavity for Slr1393g3-G.