Ontology highlight
ABSTRACT:
SUBMITTER: Prade E
PROVIDER: S-EPMC6248338 | biostudies-other | 2018 Jul
REPOSITORIES: biostudies-other
Prade Elke E Mahajan Mukesh M Im Sang-Choul SC Zhang Meng M Gentry Katherine A KA Anantharamaiah G M GM Waskell Lucy L Ramamoorthy Ayyalusamy A
Angewandte Chemie (International ed. in English) 20180614 28
Structural interactions that enable electron transfer to cytochrome-P450 (CYP450) from its redox partner CYP450-reductase (CPR) are a vital prerequisite for its catalytic mechanism. The first structural model for the membrane-bound functional complex to reveal interactions between the full-length CYP450 and a minimal domain of CPR is now reported. The results suggest that anchorage of the proteins in a lipid bilayer is a minimal requirement for CYP450 catalytic function. Akin to cytochrome-b<sub ...[more]