1. Volume 95, Issue 3, Pages 1256-1267 (August 2008)
FTIR Study of the Photoinduced Processes of Plant Phytochrome Phya using Isotope- Labeled Bilins and Density Functional Theory Calculations 
Pascale Schwinté, Harald Foerstendorf, Zakir Hussain, Wolfgang Gärtner, Maria-Andrea Mroginski, Peter Hildebrandt, Friedrich Siebert 
Biophysical Journal 
Volume 95, Issue 3, Pages (August 2008)
DOI: /biophysj
Copyright © 2008 The Biophysical Society Terms and Conditions

2. Figure 1
Structure of phytochromobilin (PΦB; R = vinyl) and phycocyanobilin (PCB; R = ethyl). Positions for 13C labeling are at C(5) and C(10). 15N labeling has been uniformly carried out at all nitrogens. In the text the individual methine bridges are denoted by A-B, B-C, and C-D.
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

3. Figure 2
Comparison of FTIR difference spectra of phyA reconstituted with nonlabeled PΦB and phyA reconstituted with uniformly 13C-labeled PΦB. The spectra of the adducts with nonlabeled and labeled PΦB are given by the gray and black lines, respectively. The spectra (from top to bottom) refer to the “Pfr” minus “Pr” (A), “lumi-R” minus “Pr” (B), and “lumi-F” minus “Pfr” (C) differences. Protein changes are denoted by an asterisk. Further details are given in the text (Materials and Methods).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

4. Figure 3
Comparison of FTIR difference spectra of phyA reconstituted with nonlabeled PΦB and phyA reconstituted with 13C(10)-labeled PΦB. The spectra of the adducts with nonlabeled and labeled PΦB are given by the gray and black lines, respectively. The spectra (from top to bottom) refer to the “Pfr” minus “Pr” (A), “lumi-R” minus “Pr” (B), and “lumi-F” minus “Pfr” (C) differences. Protein changes are denoted by an asterisk. Further details are given in the text (Materials and Methods).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

5. Figure 4
Comparison of FTIR difference spectra of phyA reconstituted with nonlabeled PΦB and phyA reconstituted with uniformly 13C(5)-labeled PCB. The spectra of the adducts with nonlabeled and labeled PΦB are given by the gray and black lines, respectively. The spectra (from top to bottom) refer to the “Pfr” minus “Pr” (A), “lumi-R” minus “Pr” (B), and “lumi-F” minus “Pfr” (C) differences. Protein changes are denoted by an asterisk. Further details are given in the text (Materials and Methods).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

6. Figure 5
Comparison of FTIR difference spectra of phyA reconstituted with nonlabeled PΦB and phyA reconstituted with uniformly 15N-labeled PCB. The spectra of the adducts with nonlabeled and labeled PΦB are given by the gray and black lines, respectively. The spectra (from top to bottom) refer to the “Pfr” minus “Pr” (A), “lumi-R” minus “Pr” (B), and “lumi-F” minus “Pfr” (C) differences. Protein changes are denoted by an asterisk. Further details are given in the text (Materials and Methods).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions

7. Figure 6
Comparison of FTIR difference spectra of phyA reconstituted with nonlabeled PΦB and phyA reconstituted with PΦB in H2O (gray) and D2O (black). The spectra (from top to bottom) refer to the “Pfr” minus “Pr” (A), “lumi-R” minus “Pr” (B), and “lumi-F” minus “Pfr” (C) differences. Protein changes are denoted by an asterisk. Further details are given in the text (Materials and Methods).
Biophysical Journal  , DOI: ( /biophysj )
Copyright © 2008 The Biophysical Society Terms and Conditions