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Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F13%3A00397877" target="_blank" >RIV/61388955:_____/13:00397877 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1021/ja406830d" target="_blank" >http://dx.doi.org/10.1021/ja406830d</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/ja406830d" target="_blank" >10.1021/ja406830d</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface

  • Original language description

    We report a new metallolabeled blue copper protein, Re126W122CuI Pseudomonas aeruginosa azurin, which has three redox sites at well-defined distances in the protein fold: ReI(CO)3(4,7-dimethyl- 1,10-phenanthroline) covalently bound at H126, a Cu center,and an indole side chain W122 situated between the Re and Cu sites (Re- W122(indole) = 13.1 ?, dmp-W122(indole) = 10.0 ?, Re-Cu = 25.6 ?). Near-UV excitation of the Re chromophore leads to prompt CuI oxidation (<50 ns), followed by slow back ET to regenerate CuI and ground-state ReI with biexponential kinetics, 220 ns and 6 ?s. From spectroscopic measurements of kinetics and relative ET yields at different concentrations, it is likely that the photoinduced ET reactions occur in protein dimers, (Re126W122CuI)2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//<-W122<-CuI, where // denotes a proteinprotein interface. Solution mass spectrometry confirms a broad oligomer distr

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CF - Physical chemistry and theoretical chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/LH13015" target="_blank" >LH13015: Metalloprotein photoactivation: Structural dynamics and electron transfer</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • 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 the American Chemical Society

  • ISSN

    0002-7863

  • e-ISSN

  • Volume of the periodical

    135

  • Issue of the periodical within the volume

    41

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    15515-15525

  • UT code for WoS article

    000326125200038

  • EID of the result in the Scopus database