ArticleBiophysical journal2003
Deuterium isotope effects in the photocycle transitions of the photoactive yellow protein.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 56 citations in OpenAlex.
- Spectrokinetic characterization of photoactive yellow protein films for integrated optical applications.European biophysics journal : EBJ · 2019Article
- Strong ionic hydrogen bonding causes a spectral isotope effect in photoactive yellow protein.Biophysical journal · 2013Article
- Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- On the involvement of single-bond rotation in the primary photochemistry of photoactive yellow protein.Biophysical journal · 2011Article
- 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
- Subpicosecond Excited-State Proton Transfer Preceding Isomerization During the Photorecovery of Photoactive Yellow Protein.The journal of physical chemistry letters · 2010Article
- Role of a conserved salt bridge between the PAS core and the N-terminal domain in the activation of the photoreceptor photoactive yellow protein.Biophysical journal · 2007Article
- The transient accumulation of the signaling state of photoactive yellow protein is controlled by the external pH.Biophysical journal · 2006Article
- Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy.Biophysical journal · 2006Article
- Predicting the signaling state of photoactive yellow protein.Biophysical journal · 2005Article
- Solvent-based deuterium isotope effects on the redox thermodynamics of cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2004Article
- Time-resolved resonance raman structural studies of the pB' intermediate in the photocycle of photoactive yellow protein.Biophysical journal · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Photoactive Yellow Protein (PYP) from Halorhodospira halophila (formerly Ectothiorhodospira halophila) is increasingly used as a model system. As such, a thorough understanding of the photocycle of PYP is essential. In this study we have combined information from pOH- (or pH-) dependence and (kinetic) deuterium isotope effects to elaborate on existing photocycle models. For several characteristics of PYP we were able to make a distinction between pH- and pOH-dependence, a nontrivial distinction when comparing data from samples dissolved in H(2)O and D(2)O. It turns out that most characteristics of PYP are pOH-dependent. We confirmed the existence of a pB' intermediate in the pR to pB transition of the photocycle. In addition, we were able to show that the pR to pB' transition is reversible, which explains the previously observed biexponential character of the pR-to-pB photocycle step. Also, the absorption spectrum of pB' is slightly red-shifted with respect to pB. The recovery of the pG state is accompanied by an inverse kinetic deuterium isotope effect. Our interpretation of this is that before the chromophore can be isomerized, it is deprotonated by a hydroxide ion from solution. From this we propose a new photocycle intermediate, pB(deprot), from which pG is recovered and which is in equilibrium with pB. This is supported in our data through the combination of the observed pOH and pH dependence, together with the kinetic deuterium isotope effect.
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