Probing protein–protein and protein–substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, b5, and reductase | Zendy

Katherine A. Gentry | Zendy; G.M. Anantharamaiah | Zendy; Ayyalusamy Ramamoorthy | Zendy

Open Access

Probing 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.

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