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
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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/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
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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