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POR protein, human

Known as: NADPH--Cytochrome P450 Reductase, EC 1.6.2.4, NADPH-Specific Cytochrome C Reductase 
NADPH-cytochrome P450 reductase (677 aa, ~77 kDa) is encoded by the human POR gene. This protein plays a role in electron transfer.
National Institutes of Health

Related topics

Related topics

10 relations
AromataseEnzyme GeneEstrogen Metabolic ProcessNADPH-ferrihemoprotein reductase activity

Broader (2)

Cytochrome P450NADPH-Ferrihemoprotein Reductase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2011
Review
2011
Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450.
Highly Cited
2011
Highly Cited
2011
Structure and Dynamics of the Membrane-Bound Cytochrome P450 2C9
The microsomal, membrane-bound, human cytochrome P450 (CYP) 2C9 is a liver-specific monooxygenase essential for drug metabolism… 
Highly Cited
2010
Highly Cited
2010
Plant NADPH-cytochrome P450 oxidoreductases.
Highly Cited
2009
Highly Cited
2009
Domain Motion in Cytochrome P450 Reductase
NADPH-cytochrome P450 reductase (CPR), a diflavin reductase, plays a key role in the mammalian P450 mono-oxygenase system. In its… 
Highly Cited
2004
Highly Cited
2004
Hypoxia Targeted Gene Therapy to Increase the Efficacy of Tirapazamine as an Adjuvant to Radiotherapy
Solid tumors are characterized by regions of hypoxia that are inherently resistant to both radiotherapy and some chemotherapy. To… 
Highly Cited
2002
Highly Cited
2002
Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding.
The kinetics of internal electron transfer in human cytochrome P450 reductase have been studied using temperature-jump relaxation… 
Highly Cited
1999
Highly Cited
1999
Biodiversity of the P450 catalytic cycle: yeast cytochrome b 5/NADH cytochrome b 5 reductase complex efficiently drives the entire sterol 14‐demethylation (CYP51) reaction
Highly Cited
1999
Highly Cited
1999
Crystal structure of the FMN‐binding domain of human cytochrome P450 reductase at 1.93 Å resolution
The crystal structure of the FMN‐binding domain of human NADPH‐cytochrome P450 reductase (P450R‐FMN), a key component in the… 
Highly Cited
1997
Highly Cited
1997
Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.
Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two mammalian enzymes known to contain both FAD and FMN, the… 
Highly Cited
1979
Highly Cited
1979
NADPH cytochrome P-450 reductase activation of quinone anticancer agents to free radicals.
With NADPH as the electron donor, rat liver NADPH cytochrome P-450 reductase (NADPH:ferricytochrome oxidoreductase, EC 1.6.2.4… 
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