TY - JOUR
T1 - A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data
AU - Ahuja, Shivani
AU - Jahr, Nicole
AU - Im, Sang Choul
AU - Vivekanandan, Subramanian
AU - Popovych, Nataliya
AU - Le Clair, Stéphanie V.
AU - Huang, Rui
AU - Soong, Ronald
AU - Xu, Jiadi
AU - Yamamoto, Kazutoshi
AU - Nanga, Ravi P.
AU - Bridges, Angela
AU - Waskell, Lucy
AU - Ramamoorthy, Ayyalusamy
PY - 2013/7/26
Y1 - 2013/7/26
N2 - Background: cytb5 modulates catalysis performed by cytsP450, in vivo and in vitro. Results: The structure of full-length cytb5 was solved by NMR, and the cytP450-binding site on cytb5 was identified by mutagenesis and NMR. Conclusion: A model of the cytb5-cytP450 complex is presented. Addition of a substrate strengthens the cytb 5-cytP450 interaction. Significance: The cytb5-cytP450 complex structure will help unravel the mechanism by which cytb5 regulates catalysis by cytP450.
AB - Background: cytb5 modulates catalysis performed by cytsP450, in vivo and in vitro. Results: The structure of full-length cytb5 was solved by NMR, and the cytP450-binding site on cytb5 was identified by mutagenesis and NMR. Conclusion: A model of the cytb5-cytP450 complex is presented. Addition of a substrate strengthens the cytb 5-cytP450 interaction. Significance: The cytb5-cytP450 complex structure will help unravel the mechanism by which cytb5 regulates catalysis by cytP450.
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U2 - 10.1074/jbc.M112.448225
DO - 10.1074/jbc.M112.448225
M3 - Article
C2 - 23709268
AN - SCOPUS:84881260822
SN - 0021-9258
VL - 288
SP - 22080
EP - 22095
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 30
ER -