Probing the ligand recognition and discrimination environment of the globin-coupled oxygen sensor protein YddV by FTIR and time-resolved step-scan FTIR spectroscopy
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10296040" target="_blank" >RIV/00216208:11310/15:10296040 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1039/c5cp01708d" target="_blank" >http://dx.doi.org/10.1039/c5cp01708d</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/c5cp01708d" target="_blank" >10.1039/c5cp01708d</a>
Alternative languages
Result language
angličtina
Original language name
Probing the ligand recognition and discrimination environment of the globin-coupled oxygen sensor protein YddV by FTIR and time-resolved step-scan FTIR spectroscopy
Original language description
YddV is a newly discovered signal transducer heme protein that recognizes O-2 and CO. Structural differences in the ligand-bound heme complex in YddV reflect variations in catalytic regulation by O2 and CO. Time-resolved step-scan (TRS2) FTIR studies ofthe wild type and of the important in oxygen recognition and stability of the heme Fe(II)-O-2 complex L65M, L65T, Y43A, Y43F and Y43W mutants were performed to determine the site-specific protein dynamics following carbon monoxide (CO) photodissociation.These mutations were designed to perturb the electrostatic field near the iron-bound gaseous ligand (CO) and also to allow us to investigate the communication pathway between the distal residues of the protein and heme. TRS2-FTIR spectra of YddV-heme-COshow that the heme propionates are in protonated and deprotonated states. Moreover, the rate of decay of the vibrations of amide I is on a time scale that coincides with the rate of rebinding of CO, which suggests that there is coupling
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA15-19883S" target="_blank" >GA15-19883S: Molecular mechanisms of intraprotein/interdomain signal transduction in model heme sensor proteins</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Physical Chemistry Chemical Physics
ISSN
1463-9076
e-ISSN
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Volume of the periodical
17
Issue of the periodical within the volume
26
Country of publishing house
GB - UNITED KINGDOM
Number of pages
9
Pages from-to
17007-17015
UT code for WoS article
000356874000041
EID of the result in the Scopus database
2-s2.0-84933060391