Ultrafast Spectroscopy Evidence for Picosecond Ligand Exchange at the Binding Site of a Herne Protein: Heme-Based Sensor YddV
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F16%3A10323477" target="_blank" >RIV/00216208:11310/16:10323477 - isvavai.cz</a>
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=pLgNpL6KiK" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=pLgNpL6KiK</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jpclett.5b02517" target="_blank" >10.1021/acs.jpclett.5b02517</a>
Alternative languages
Result language
angličtina
Original language name
Ultrafast Spectroscopy Evidence for Picosecond Ligand Exchange at the Binding Site of a Herne Protein: Heme-Based Sensor YddV
Original language description
An important question for the functioning of heme proteins is whether different ligands present within the protein moiety can readily exchange with heme-bound ligands. Studying the dynamics of the heme domain of the Escherichia coli sensor protein YddV upon dissociation of NO from the ferric heme by ultrafast spectroscopy, we demonstrate that when the hydrophobic leucine residue in the distal heme pocket is mutated to glycine, in a substantial fraction of the protein water replaces NO as an internal ligand in as fast as similar to 4 ps. This process, which is near-barrierless and occurs orders of magnitude faster than the corresponding process in myoglobin, corresponds to a ligand swap of NO with a water molecule present in the heme pocket, as corroborated by molecular dynamics simulations. Our findings provide important new insight into ligand exchange in heme proteins that functionally interact with different external ligands.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
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
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Physical Chemistry Letters
ISSN
1948-7185
e-ISSN
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Volume of the periodical
7
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
69-74
UT code for WoS article
000367968700013
EID of the result in the Scopus database
2-s2.0-84954165580