Photo-initiated crosslinking extends mapping of the protein-protein interface to membrane-embedded portions of cytochromes P450 2B4 and b5
Identifikátory výsledku
Kód výsledku v 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>
Nalezeny alternativní kódy
RIV/61388971:_____/15:00456041
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Photo-initiated crosslinking extends mapping of the protein-protein interface to membrane-embedded portions of cytochromes P450 2B4 and b5
Popis výsledku v původním jazyce
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
Název v anglickém jazyce
Photo-initiated crosslinking extends mapping of the protein-protein interface to membrane-embedded portions of cytochromes P450 2B4 and b5
Popis výsledku anglicky
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
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
<a href="/cs/project/GAP207%2F12%2F0627" target="_blank" >GAP207/12/0627: INTERAKCE SAVČÍHO MIKROSOMÁLNÍHO CYTOCHROMU P450 S REDOX PARTNERY - TOPOLOGIE A STRUKTURNĚ-FUNKČNÍ VZTAHY</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Methods
ISSN
1046-2023
e-ISSN
—
Svazek periodika
89
Číslo periodika v rámci svazku
November 2015
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
10
Strana od-do
128-137
Kód UT WoS článku
000365062800016
EID výsledku v databázi Scopus
2-s2.0-84946496797