Ontology highlight
ABSTRACT:
SUBMITTER: Sugishima M
PROVIDER: S-EPMC3932878 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Sugishima Masakazu M Sato Hideaki H Higashimoto Yuichiro Y Harada Jiro J Wada Kei K Fukuyama Keiichi K Noguchi Masato M
Proceedings of the National Academy of Sciences of the United States of America 20140203 7
NADPH-cytochrome P450 oxidoreductase (CPR) supplies electrons to various heme proteins including heme oxygenase (HO), which is a key enzyme for heme degradation. Electrons from NADPH flow first to flavin adenine dinucleotide, then to flavin mononucleotide (FMN), and finally to heme in the redox partner. For electron transfer from CPR to its redox partner, the ''closed-open transition'' of CPR is indispensable. Here, we demonstrate that a hinge-shortened CPR variant, which favors an open conforma ...[more]