Results 31 to 40 of about 61 (60)
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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
Daniel S. Sem, Charles B. Kasper
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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
Daniel S. Sem, Charles B. Kasper
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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.
Terrence R. Green, David E. Wu
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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.
Terrence R. Green, David E. Wu
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Archives of Biochemistry and Biophysics, 1982
Abstract Various flavin analogs were used as alternate substrates or competitive inhibitors to characterize the FMN binding sites of the NADH- and NADPH-specific FMN oxidoreductases from Beneckea harveyi . Several polyhydroxyl compounds were found to be poor competitive inhibitors for the FMN sites of these enzymes.
B. Nefsky, Marlene DeLuca
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Abstract Various flavin analogs were used as alternate substrates or competitive inhibitors to characterize the FMN binding sites of the NADH- and NADPH-specific FMN oxidoreductases from Beneckea harveyi . Several polyhydroxyl compounds were found to be poor competitive inhibitors for the FMN sites of these enzymes.
B. Nefsky, Marlene DeLuca
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Etude des activités NADH et NADPH-ferrédoxine oxydoréductasiques chez Clostridium acetobutylicum
Canadian Journal of Microbiology, 1977The 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
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Biochemistry, 1978
Highly purified NADH and NADPH:FMN oxidoreductases from Beneckea harveyi have been characterized with regard to kinetic parameters, association with luciferase, activity with artificial electron acceptors, and the effects of inhibitors. The NADH:FMN oxidoreductase exhibits single displacement kinetics while the NADPH:FMN oxidoreductase exhibits double ...
Marlene DeLuca, Edward Jablonski
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Highly purified NADH and NADPH:FMN oxidoreductases from Beneckea harveyi have been characterized with regard to kinetic parameters, association with luciferase, activity with artificial electron acceptors, and the effects of inhibitors. The NADH:FMN oxidoreductase exhibits single displacement kinetics while the NADPH:FMN oxidoreductase exhibits double ...
Marlene DeLuca, Edward Jablonski
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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
James E. Krause, Harry J. Karavolas
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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
James E. Krause, Harry J. Karavolas
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Journal of Molecular Biology, 1999
Respiratory chains of bacteria and mitochondria contain closely related forms of the proton-pumping NADH:ubiquinone oxidoreductase, or complex I. The bacterial complex I consists of 14 subunits, whereas the mitochondrial complex contains some 25 extra subunits in addition to the homologues of the bacterial subunits.
Wolfgang Fecke +7 more
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Respiratory chains of bacteria and mitochondria contain closely related forms of the proton-pumping NADH:ubiquinone oxidoreductase, or complex I. The bacterial complex I consists of 14 subunits, whereas the mitochondrial complex contains some 25 extra subunits in addition to the homologues of the bacterial subunits.
Wolfgang Fecke +7 more
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
The reduction of NADH:Q oxidoreductase by NADPH occurring in submitochondrial particles has been studied with the freeze-quench technique. It was found that 50% of the Fe-S clusters 2, 3 and 4 could be reduced by NADPH within 30 ms at pH 6.5. The remainder of the clusters, including cluster 1, were reduced slowly and incompletely; it was concluded that
P.T.A. Bakker, Simon P. J. Albracht
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The reduction of NADH:Q oxidoreductase by NADPH occurring in submitochondrial particles has been studied with the freeze-quench technique. It was found that 50% of the Fe-S clusters 2, 3 and 4 could be reduced by NADPH within 30 ms at pH 6.5. The remainder of the clusters, including cluster 1, were reduced slowly and incompletely; it was concluded that
P.T.A. Bakker, Simon P. J. Albracht
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[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].
Canadian journal of microbiology, 1977The 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
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Activity‐Based Protein Profiling (ABPP) of Oxidoreductases
ChemBioChem, 2021Rolf Breinbauer, Hrudayanath Thatoi
exaly