Journal of Physical Chemistry B, volume 125, issue 22, pages 5874-5884

Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects.

Koeppe Benjamin 1
, 
Tolstoy Peter M. 2
, 
Guo Jing 3
, 
Denisov Gleb S. 4
, 
LIMBACH H. G. 5
1
 
J. Heyrovský Institute of Physical Chemistry, Dolejškova 2155/3, 182 23 Prague 8, Czech Republic | 
2
 
3
 
Department of Radiology, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany | 
4
 
5
 
Publication type: Journal Article
Publication date: 2021-06-01
Quartile SCImago
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Impact factor: 3.3
ISSN: 15206106, 15205207
Materials Chemistry
Surfaces, Coatings and Films
Physical and Theoretical Chemistry
Abstract
Intramolecular hydrogen bonds in aprotic media were studied by combined (simultaneous) NMR and UV-vis spectroscopy. The species under investigation were anionic and featured single or coupled H-bonds between, for example, carboxylic groups and phenolic oxygen atoms (COO···H···OC)-, among phenolic oxygen atoms (CO···H···OC)-, and hydrogen bond chains between a carboxylic group and two phenolic oxygen atoms (COO···H···(OC)···H···OC)-. The last anion may be regarded as a small molecule model for the hydrogen bond system in the active site of wild-type photoactive yellow protein (PYP) while the others mimic the corresponding H-bonds in site-selective mutants. Proton positions in isolated hydrogen bonds and hydrogen bond chains were assessed by calculations for vacuum conditions and spectroscopically for the two media, CD2Cl2 and the liquefied gas mixture CDClF2/CDF3 at low temperatures. NMR parameters allow for the estimation of time-averaged H-bond geometries, and optical spectra give additional information about geometry distributions. Comparison of the results from the various systems revealed the effects of the formation of hydrogen bond chains and changes of medium conditions on the geometry of individual H-bonds. In particular, the proton in a hydrogen bond to a carboxylic group shifts from the phenolic oxygen atom in the system COO-···H-OC to the carboxylic group in COO-H···(OC)-···H-OC as a result of hydrogen bond formation to the additional phenolic donor. Increase in medium polarity may, however, induce the conversion of a structure of a type COO-H···(OC)-···H-OC to the type COO-···H-(OC)···H-OC. Application of these results obtained from the model systems to PYP suggests that both cooperative effects within the hydrogen bond chain and a low-polarity protein environment are prerequisites for the stabilization of negative charge on the cofactor and hence for the spectral tuning of the photoreceptor.
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Koeppe B. et al. Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects. // Journal of Physical Chemistry B. 2021. Vol. 125. No. 22. pp. 5874-5884.
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Koeppe B., Tolstoy P. M., Guo J., Denisov G. S., LIMBACH H. G. Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects. // Journal of Physical Chemistry B. 2021. Vol. 125. No. 22. pp. 5874-5884.
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TY - JOUR
DO - 10.1021/acs.jpcb.0c09923
UR - https://doi.org/10.1021%2Facs.jpcb.0c09923
TI - Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects.
T2 - Journal of Physical Chemistry B
AU - Koeppe, Benjamin
AU - Tolstoy, Peter M.
AU - LIMBACH, H. G.
AU - Guo, Jing
AU - Denisov, Gleb S.
PY - 2021
DA - 2021/06/01 00:00:00
PB - American Chemical Society (ACS)
SP - 5874-5884
IS - 22
VL - 125
SN - 1520-6106
SN - 1520-5207
ER -
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@article{2021_Koeppe,
author = {Benjamin Koeppe and Peter M. Tolstoy and H. G. LIMBACH and Jing Guo and Gleb S. Denisov},
title = {Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects.},
journal = {Journal of Physical Chemistry B},
year = {2021},
volume = {125},
publisher = {American Chemical Society (ACS)},
month = {jun},
url = {https://doi.org/10.1021%2Facs.jpcb.0c09923},
number = {22},
pages = {5874--5884},
doi = {10.1021/acs.jpcb.0c09923}
}
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Koeppe, Benjamin, et al. “Combined NMR and UV-Vis Spectroscopic Studies of Models for the Hydrogen Bond System in the Active Site of Photoactive Yellow Protein: H-Bond Cooperativity and Medium Effects..” Journal of Physical Chemistry B, vol. 125, no. 22, Jun. 2021, pp. 5874-5884. https://doi.org/10.1021%2Facs.jpcb.0c09923.
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