Document Detail

Conformational homogeneity and excited-state isomerization dynamics of the bilin chromophore in phytochrome Cph1 from resonance Raman intensities.
MedLine Citation:
PMID:  22325295     Owner:  NLM     Status:  MEDLINE    
The ground-state structure and excited-state isomerization dynamics of the P(r) and P(fr) forms of phytochrome Cph1 are investigated using resonance Raman intensity analysis. Electronic absorption and stimulated resonance Raman spectra of P(r) and P(fr) are presented; vibronic analysis of the Raman intensities and absorption spectra reveals that both conformers exist as a single, homogeneous population of molecules in the ground state. The homogeneous and inhomogeneous contributions to the overall electronic broadening are determined, and it is found that the broadening is largely homogeneous in nature, pointing to fast excited-state decay. Franck-Condon displacements derived from the Raman intensity analysis reveal the initial atomic motions in the excited state, including the highly displaced, nontotally symmetric torsional and C(15)-H HOOP modes that appear because of symmetry-reducing distortions about the C(14)-C(15) and C(15)=C(16) bonds. P(fr) is especially well primed for ultrafast isomerization and torsional Franck-Condon analysis predicts a <200 fs P(fr) → P(r) isomerization. This time is significantly faster than the observed 700 fs reaction time, indicating that the P(fr) S(1) surface has a D-ring rotational barrier caused by steric interactions with the protein.
Katelyn M Spillane; Jyotishman Dasgupta; Richard A Mathies
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-02-07
Journal Detail:
Title:  Biophysical journal     Volume:  102     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-02-13     Completed Date:  2012-06-15     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  709-17     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Department of Chemistry, University of California, Berkeley, California, USA.
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MeSH Terms
Bile Pigments / chemistry*
Molecular Conformation*
Phytochrome / chemistry*
Spectrum Analysis, Raman*
Reg. No./Substance:
0/Bile Pigments; 11121-56-5/Phytochrome

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