Membrane-attached mammalian cytochromes P450: An overview of the membrane's effects on structure, drug binding, and interactions with redox partners
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F18%3A73588834" target="_blank" >RIV/61989592:15110/18:73588834 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/18:73588834
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0162013417308413" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0162013417308413</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jinorgbio.2018.03.002" target="_blank" >10.1016/j.jinorgbio.2018.03.002</a>
Alternative languages
Result language
angličtina
Original language name
Membrane-attached mammalian cytochromes P450: An overview of the membrane's effects on structure, drug binding, and interactions with redox partners
Original language description
Mammalian cytochromes P450 are an important class of enzymes involved in the biotransformation of many endo- and exogenous compounds. Cytochrome P450 isoforms are attached to the membrane of the endoplasmic reticulum or mitochondria, and their catalytic domains move along the membrane surface while being partially immersed in the membrane environment. Their active sites are connected to both the membrane and cytosolic environments via a complex network of access channels. Consequently, they can accept substrates from both environments. The membrane also supports the interactions of cytochromes P450 with their redox partners. In this review, we provide an overview of current knowledge of the structure, flexibility, and interactions with substrates and redox partners of cytochrome P450 on membranes, amalgamating information derived from both experiments and simulations.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
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 INORGANIC BIOCHEMISTRY
ISSN
0162-0134
e-ISSN
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Volume of the periodical
183
Issue of the periodical within the volume
JUN
Country of publishing house
US - UNITED STATES
Number of pages
20
Pages from-to
117-136
UT code for WoS article
000432233100013
EID of the result in the Scopus database
2-s2.0-85045083695