Results 131 to 140 of about 8,969 (152)
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Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH

Biochemistry, 1993
Site-directed mutagenesis has been used in conjunction with pH and alternate substrate/inhibitor studies to characterize the interactions between NADPH-cytochrome P-450 oxidoreductase (P-450R) and the 2'-phosphate of NADP(H) that provide P-450R with its strong nicotinamide nucleotide specificity. It is known that the 2'-phosphate of NADP(H) is bound to
D S, Sem, C B, Kasper
openaire   +2 more sources

Purification and resolution of NADH diaphorase activity from NADPH diaphorase-linked: O2 oxidoreductase activity of human neutrophils

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Intrinsic NADPH diaphorase activity is a component of the membrane-bound NAD(P)H:O2 oxidoreductase of human neutrophils. NADH-specific diaphorase activity is also present in membrane fractions rich in oxidoreductase activity. Studies were undertaken to determine whether the NADH diaphorase might also be intrinsic to the oxidoreductase.
T R, Green, D E, Wu
openaire   +2 more sources

Subcellular location of hypothalamic progesterone metabolizing enzymes and evidence for distinct NADH- and NADHP-linked 3α-hydroxysteroid oxidoreductase activities

Journal of Steroid Biochemistry, 1980
Abstract The subcellular location of adult female rat hypothalamic steroid 5α-reductase and 3α-hydroxysteroid oxidoreductase (3α-HSD) activities, which catalyze the conversion of progesterone to 3α-hydroxy-5α-pregnan-20-one via 5α-pregnane-3,20-dione, have been investigated using 3 H-labeled substrates and an isotopic dilution assay system. In crude
J E, Krause, H J, Karavolas
openaire   +2 more sources

[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].

Canadian journal of microbiology, 1977
The NADH and NADPH-ferredoxin oxidoreductase have been studied in Clostridium acetobutylicum. Acetyl-CoA is an obligatory activator of NADH-ferredoxin reductase activity and NADH a competitive inhibitor of ferredoxin-NAD+ reductase activity. These regulations are the same when C.
H, Petitdemange   +3 more
openaire   +1 more source

InspIRED by Nature: NADPH‐Dependent Imine Reductases (IREDs) as Catalysts for the Preparation of Chiral Amines

Chemistry - A European Journal, 2016
Gideon James Grogan, Nicholas J Turner
exaly  

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