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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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