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Membrane-attached mammalian cytochromes P450: An overview of the membrane's effects on structure, drug binding, and interactions with redox partners.

Authors :
Šrejber M
Navrátilová V
Paloncýová M
Bazgier V
Berka K
Anzenbacher P
Otyepka M
Source :
Journal of inorganic biochemistry [J Inorg Biochem] 2018 Jun; Vol. 183, pp. 117-136. Date of Electronic Publication: 2018 Mar 05.
Publication Year :
2018

Abstract

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.<br /> (Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1873-3344
Volume :
183
Database :
MEDLINE
Journal :
Journal of inorganic biochemistry
Publication Type :
Academic Journal
Accession number :
29653695
Full Text :
https://doi.org/10.1016/j.jinorgbio.2018.03.002