NADPH P450 oxidoreductase: structure, function, and pathology of diseases

AV Pandey, CE Flück - Pharmacology & therapeutics, 2013 - Elsevier
Cytochrome P450 oxidoreductase (POR) is an enzyme that is essential for multiple
metabolic processes, chiefly among them are reactions catalyzed by cytochrome P450 …

Molecular mechanism of phase I and phase II drug‐metabolizing enzymes: implications for detoxification

T Iyanagi - International review of cytology, 2007 - Elsevier
Enzymes that catalyze the biotransformation of drugs and xenobiotics are generally referred
to as drug‐metabolizing enzymes (DMEs). DMEs can be classified into two main groups …

Structure and mechanism of the complex between cytochrome P4503A4 and ritonavir

IF Sevrioukova, TL Poulos - Proceedings of the National Academy of …, 2010 - pnas.org
Ritonavir is a HIV protease inhibitor routinely prescribed to HIV patients that also potently
inactivates cytochrome P4503A4 (CYP3A4), the major human drug-metabolizing enzyme …

Second‐coordination sphere effects on selectivity and specificity of heme and nonheme iron enzymes

SP de Visser - Chemistry–A European Journal, 2020 - Wiley Online Library
Mononuclear iron‐containing enzymes are highly versatile oxidants that often react
stereospecifically and/or regioselectively with substrates. Combined experimental and …

Plant NADPH-cytochrome P450 oxidoreductases

K Jensen, BL Møller - Phytochemistry, 2010 - Elsevier
NADPH-cytochrome P450 oxidoreductase (CPR) serves as the electron donor to almost all
eukaryotic cytochromes P450. It belongs to a small family of diflavin proteins and is built of …

Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human …

H Olteanu, T Munson, R Banerjee - Biochemistry, 2002 - ACS Publications
Methionine synthase reductase (MSR) catalyzes the conversion of the inactive form of
human methionine synthase to the active state of the enzyme. This reaction is of paramount …

Electron transfer by diflavin reductases

MB Murataliev, R Feyereisen, FA Walker - Biochimica et Biophysica Acta …, 2004 - Elsevier
Diflavin reductases are enzymes which emerged as a gene fusion of ferredoxin (flavodoxin)
reductase and flavodoxin. The enzymes of this family tightly bind two flavin cofactors, FAD …

NADPH–cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family

T Iyanagi, C **a, JJP Kim - Archives of biochemistry and biophysics, 2012 - Elsevier
NADPH–cytochrome P450 oxidoreductase (CYPOR) and nitric oxide synthase (NOS), two
members of the diflavin oxidoreductase family, are multi-domain enzymes containing distinct …

[HTML][HTML] Biochemical and structural insights into bacterial organelle form and biogenesis

JB Parsons, SD Dinesh, E Deery, HK Leech… - Journal of biological …, 2008 - Elsevier
Many heterotrophic bacteria have the ability to make polyhedral structures containing
metabolic enzymes that are bounded by a unilamellar protein shell (metabolosomes or …

Nitric-oxide synthase: a cytochrome P450 family foster child

ACF Gorren, B Mayer - Biochimica et Biophysica Acta (BBA)-General …, 2007 - Elsevier
Nitric-oxide synthase (NOS), the enzyme responsible for mammalian NO generation, is no
cytochrome P450, but there are striking similarities between both enzymes. First and …