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Photo-initiated crosslinking extends mapping of the protein-protein interface to membrane-embedded portions of cytochromes P450 2B4 and b5

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10306942" target="_blank" >RIV/00216208:11310/15:10306942 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/15:00456041

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.ymeth.2015.07.015" target="_blank" >http://dx.doi.org/10.1016/j.ymeth.2015.07.015</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ymeth.2015.07.015" target="_blank" >10.1016/j.ymeth.2015.07.015</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Photo-initiated crosslinking extends mapping of the protein-protein interface to membrane-embedded portions of cytochromes P450 2B4 and b5

  • Original language description

    Protein-protein interactions play a central role in the regulation of many biochemical processes (e.g. the system participating in enzyme catalysis). Therefore, a deeper understanding of protein-protein interactions may contribute to the elucidation ofmany biologically important mechanisms. For this purpose, it is necessary to establish the composition and stoichiometry of supramolecular complexes and to identify the crucial portions of the interacting molecules. This study is devoted to structure-functional relationships in the microsomal Mixed Function Oxidase (MFO) complex, which is responsible for biotransformation of many hydrophobic endogenous compounds and xenobiotics. In particular, the cytochrome b5 interaction with MFO terminal oxygenase cytochrome P-450 (P450) was studied. To create photolabile probes suitable for this purpose, we prepared cytochrome b5 which had a photolabile diazirine analog of methionine (pMet) incorporated into the protein sequence, employing recombinant

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP207%2F12%2F0627" target="_blank" >GAP207/12/0627: MAMMALIAN MICROSOMAL CYTOCHROME P450 INTERACTION WITH REDOX PARTNERS - TOPOLOGY AND STRUCTURE-FUNCTION RELATIONSHIPS</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

    Methods

  • ISSN

    1046-2023

  • e-ISSN

  • Volume of the periodical

    89

  • Issue of the periodical within the volume

    November 2015

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    128-137

  • UT code for WoS article

    000365062800016

  • EID of the result in the Scopus database

    2-s2.0-84946496797