Results 1 to 10 of about 160,314 (244)
Structural Features of Cytochrome b5–Cytochrome b5 Reductase Complex Formation and Implications for the Intramolecular Dynamics of Cytochrome b5 Reductase [PDF]
International Journal of Molecular Sciences, 2021 Membrane cytochrome b5 reductase is a pleiotropic oxidoreductase that uses primarily soluble reduced nicotinamide adenine dinucleotide (NADH) as an electron donor to reduce multiple biological acceptors localized in cellular membranes. Some of the biological acceptors of the reductase and coupled redox proteins might eventually transfer electrons to ...
Carlos Gutiérrez-Merino +3 more
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Measurement of cytochrome P450 and NADPH–cytochrome P450 reductase [PDF]
Nature Protocols, 2009 Cytochrome P450 (P450) enzymes are important in the metabolism of steroids, vitamins, carcinogens, drugs and other compounds. Two of the commonly used assays in this field are the measurements of total P450 and NADPH-P450 reductase in biological preparations. A detailed protocol is presented for the measurement of P450 by its spectral properties, along
F Peter, Guengerich +3 more
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Nitrite Reductase Activity of Cytochrome c [PDF]
Journal of Biological Chemistry, 2008 Small increases in physiological nitrite concentrations have now been shown to mediate a number of biological responses, including hypoxic vasodilation, cytoprotection after ischemia/reperfusion, and regulation of gene and protein expression. Thus, while nitrite was until recently believed to be biologically inert, it is now recognized as a potentially
Swati, Basu +7 more
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Puzzling subunits of mitochondrial cytochrome reductase [PDF]
Trends in Biochemical Sciences, 1990 The ubiquinol-cytochrome c reductase complex, like the other proton-pumping respiratory complexes of mitochondria, is an assembly of many different subunits. However, only a few of these subunits participate directly in the electron transfer and proton translocation. The roles of the other subunits are largely unknown.
Weiss, Hanns +2 more
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Methemoglobin Reductase (Cytochrome b5 Reductase) Deficiency in Congenital Methemoglobinemia [PDF]
Blood, 1974 Abstract Two NADH diaphorases, diaphorase I and II, were isolated from normal red cells and congenital methemoglobinemic red cells by CM-cellulose and DE 32 column chromatography. For methemoglobinemic sample, activities of diaphorase I and diaphorase II were 80% and less than 5% of those for the normal red cells, respectively.
T, Kitao +3 more
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7-Dehydrocholesterol reductase activity is independent of cytochrome P450 reductase [PDF]
The Journal of Steroid Biochemistry and Molecular Biology, 2011 7-Dehydrocholesterol reductase (DHCR7) catalyzes the final step in cholesterol synthesis. The enzyme utilizes NADPH as a source of electrons and has been reported to require NADPH-cytochrome P450 reductase (POR) as its redox partner. To test this hypothesis, microsomes were prepared from the livers of mice in which hepatic cytochrome P450 reductase ...
Ling, Zou, Li, Li, Todd D, Porter
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Cytochrome P450 2S1 is Reduced by NADPH-Cytochrome P450 Reductase [PDF]
Drug Metabolism and Disposition, 2011 Cytochrome P450 (P450) 2S1 is one of the orphan P450s without a clear physiological function. Controversy has arisen as to whether it can interact with NADPH-P450 reductase and accept electrons. The reduction of 1,4-bis{[2-(dimethylamino-N-oxide)ethyl]amino}-5,8-dihydroxyanthracene-9,10-dione (AQ4N) by P450 2S1 was confirmed, and the NADPH consumption ...
Yi, Xiao +2 more
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The cytochrome bd respiratory oxygen reductases
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2011 Cytochrome bd is a respiratory quinol: O₂ oxidoreductase found in many prokaryotes, including a number of pathogens. The main bioenergetic function of the enzyme is the production of a proton motive force by the vectorial charge transfer of protons. The sequences of cytochromes bd are not homologous to those of the other respiratory oxygen reductases ...
Borisov, Vitaliy B. +3 more
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Cytochrome P450 reductase (POR) as a ferroptosis fuel [PDF]
Protein & Cell, 2021 Koppula, Pranavi, Zhuang, Li, Gan, Boyi
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