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Biology Articles » Biophysics » Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor » Figures
Figures
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Figure 1 X-ray structure of the R. sphaeroides AppA BLUF domain. (A and B) Close-ups of the vicinity of the FAD chromophore in two proposed orientations of the conserved Gln in dark state (A) and light state (B). The coordinates were taken from Protein Data Bank ID code 1YRX (11). (Click image to enlarge) |
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Figure 2
EADS and their corresponding lifetimes resulting from global analysis of ultrafast transient absorption experiments on the Synechocystis Slr1694 BLUF domain upon excitation at 400 nm in H2O buffer (A) and in D2O buffer (B). (Click image to enlarge) |
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Figure 3
Kinetic traces of the Synechocystis Slr1694 BLUF domain in H2O (open circles) and D2O (filled circles) upon excitation at 400 nm, with detection at 483 nm (A), 550 nm (B), 610 nm (C), and 710 nm (D).
The solid lines denote the result of the target analysis. Note that the
time axis is linear from −10 to 20 ps and logarithmic thereafter. (Click image to enlarge) |
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Figure 4
Target analysis and photocycle scheme of the Synechocystis Slr1694 BLUF domain. (Upper)
SADS of the various molecular species in the kinetic scheme that result
from the application of a target analysis to the ultrafast
time-resolved data of the Synechocystis Slr1694 BLUF domain in H2O (solid lines) and D2O (dotted lines), with FAD* (blue), Q1 (black), Q2 (magenta), and the long-lived signaling state SlrRED (orange). (Lower)
The photocycle scheme of Slr1694, with time constants as they follow
from the target analysis and assignments of the intermediate states as
described in the text. (Click image to enlarge) |
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Figure 5
The proposed reaction mechanism for photoinduced hydrogen-bond switching in the Synechocystis Slr1694 BLUF domain. See text for details. (Click image to enlarge) |
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