Open AccessProbing protein–protein and protein–substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, b5, and reductase
Author(s) -
Katherine A. Gentry,
G.M. Anantharamaiah,
Ayyalusamy Ramamoorthy
Publication year - 2019
Publication title -
chemical communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.837
H-Index - 333
eISSN - 1364-548X
pISSN - 1359-7345
DOI - 10.1039/c9cc05904k
Subject(s) - cytochrome p450 reductase , chemistry , reductase , ternary complex , cytochrome p450 , ternary operation , substrate (aquarium) , redox , membrane protein , biochemistry , substrate specificity , cytochrome , membrane , enzyme , stereochemistry , cytochrome c , biology , coenzyme q – cytochrome c reductase , mitochondrion , organic chemistry , computer science , ecology , programming language
Cytochrome P450 (cytP450) interacts with two redox partners, cytP450 reductase and cytochrome-b 5 , to metabolize substrates. Using NMR, we reveal changes in the dynamic interplay when all three proteins are incorporated into lipid nanodiscs in the absence and presence of substrates.