ArticleBiophysical journal2004
Time-resolved resonance raman structural studies of the pB' intermediate in the photocycle of photoactive yellow protein.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Photoactive Yellow Protein Represents a Distinct, Evolutionarily Novel Family of PAS Domains.Journal of bacteriology · 2022Article
- Simulations of Two-dimensional Infrared and Stimulated Resonance Raman Spectra of Photoactive Yellow Protein.Chemical physics · 2013Article
- Single-molecule vibrational spectroscopy adds structural resolution to the optical trap.Biophysical journal · 2013Article
- Protein conformational switches: from nature to design.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Review
- Energetics of short hydrogen bonds in photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Predicting the reaction coordinates of millisecond light-induced conformational changes in photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Catching a protein in the act.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Low-barrier hydrogen bond in photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The transient accumulation of the signaling state of photoactive yellow protein is controlled by the external pH.Biophysical journal · 2006Article
- Predicting the signaling state of photoactive yellow protein.Biophysical journal · 2005Article
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4 authors.
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Abstract
Time-resolved resonance Raman spectroscopy is used to obtain chromophore vibrational spectra of the pR, pB', and pB intermediates during the photocycle of photoactive yellow protein. In the pR spectrum, the C8-C9 stretching mode at 998 cm(-1) is approximately 60 cm(-1) lower than in the dark state, and the combination of C-O stretching and C7H=C8H bending at 1283 cm(-1) is insensitive to D2O substitution. These results indicate that pR has a deprotonated, cis chromophore structure and that the hydrogen bonding to the chromophore phenolate oxygen is preserved and strengthened in the early photoproduct. However, the intense C7H=C8H hydrogen out-of-plane (HOOP) mode at 979 cm(-1) suggests that the chromophore in pR is distorted at the vinyl and adjacent C8-C9 bonds. The formation of pB' involves chromophore protonation based on the protonation state marker at 1174 cm(-1) and on the sensitivity of the COH bending at 1148 cm(-1) as well as the combined C-OH stretching and C7H=C8H bending mode at 1252 cm(-1) to D2O substitution. The hydrogen out-of-plane Raman intensity at 985 cm(-1) significantly decreases in pB', suggesting that the pR-to-pB' transition is the stage where the stored photon energy is transferred from the distorted chromophore to the protein, producing a more relaxed pB' chromophore structure. The C=O stretching mode downshifts from 1660 to 1651 cm(-1) in the pB'-to-pB transition, indicating the reformation of a hydrogen bond to the carbonyl oxygen. Based on reported x-ray data, this suggests that the chromophore ring flips during the transition from pB' to pB. These results confirm the existence and importance of the pB' intermediate in photoactive yellow protein receptor activation.
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