Characterization of a Fusion Protein between Human Cytochrome P450 1A1 and Rat NADPH-P450 Oxidoreductase inEscherichia coli

1997 ◽  
Vol 230 (1) ◽  
pp. 211-214 ◽  
Author(s):  
Young Jin Chun ◽  
Tae Cheon Jeong ◽  
Jung Koo Roh ◽  
F.Peter Guengerich
Keyword(s):  
Cytochrome P450 ◽  
Fusion Protein ◽  
Inescherichia Coli ◽  
Cytochrome P450 1A1 ◽  
P450 Oxidoreductase ◽  
Human Cytochrome

Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4421-4427 ◽  
Author(s):  
Angela Wilks ◽  
Stephen M. Black ◽  
Walter L. Miller ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Cytochrome P450 ◽  
Fusion Protein ◽  
Heme Oxygenase ◽  
Cytochrome P450 Reductase ◽  
P450 Reductase ◽  
Human Cytochrome

Characterization of the Gly45Asp variant of human cytochrome P450 1A1 using recombinant expression

2015 ◽  
Vol 239 (2) ◽  
pp. 81-89 ◽  
Author(s):  
Seung Heon Lee ◽  
Hee Jeong Yu ◽  
Seungwoo Lee ◽  
Doug-Young Ryu
Keyword(s):  
Cytochrome P450 ◽  
Recombinant Expression ◽  
Cytochrome P450 1A1 ◽  
Human Cytochrome

scholarly journals An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Goutam Mukherjee ◽  
Prajwal P. Nandekar ◽  
Rebecca C. Wade
Keyword(s):  
Electron Transfer ◽  
Cytochrome P450 ◽  
Drug Targets ◽  
Catalytic Domain ◽  
Cytochrome P450 1A1 ◽  
P450 Oxidoreductase ◽  
Distal Side ◽  
Cytochrome P450 Oxidoreductase ◽  
Membrane Bound ◽  
Transient Interactions

AbstractCytochrome P450 (CYP) heme monooxygenases require two electrons for their catalytic cycle. For mammalian microsomal CYPs, key enzymes for xenobiotic metabolism and steroidogenesis and important drug targets and biocatalysts, the electrons are transferred by NADPH-cytochrome P450 oxidoreductase (CPR). No structure of a mammalian CYP–CPR complex has been solved experimentally, hindering understanding of the determinants of electron transfer (ET), which is often rate-limiting for CYP reactions. Here, we investigated the interactions between membrane-bound CYP 1A1, an antitumor drug target, and CPR by a multiresolution computational approach. We find that upon binding to CPR, the CYP 1A1 catalytic domain becomes less embedded in the membrane and reorients, indicating that CPR may affect ligand passage to the CYP active site. Despite the constraints imposed by membrane binding, we identify several arrangements of CPR around CYP 1A1 that are compatible with ET. In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. Computed ET rates and pathways agree well with available experimental data and suggest why the CYP–CPR ET rates are low compared to those of soluble bacterial CYPs.

Characterization of Diuron N-Demethylation by Mammalian Hepatic Microsomes and cDNA-Expressed Human Cytochrome P450 Enzymes

2007 ◽  
Vol 35 (9) ◽  
pp. 1634-1641 ◽  
Author(s):  
Khaled Abass ◽  
Petri Reponen ◽  
Miia Turpeinen ◽  
Jorma Jalonen ◽  
Olavi Pelkonen
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzymes ◽  
Hepatic Microsomes ◽  
Human Cytochrome
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