Results 261 to 270 of about 23,312 (291)

Reduction of cytochrome b5 by NADPH–cytochrome P450 reductase

Archives of Biochemistry and Biophysics, 2005
The reduction of mammalian cytochrome b5 (b5) by NADPH-cytochrome P450 (P450) reductase is involved in a number of biological reactions. The kinetics of the process have received limited consideration previously, and a combination of pre-steady-state (stopped-flow) and steady-state approaches was used to investigate the mechanism of b5 reduction.
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Electron transfer in human cytochrome P450 reductase

Biochemical Society Transactions, 2003
Cytochrome P450 reductase (CPR) is a diflavin enzyme responsible for electron donation to mammalian cytochrome P450 enzymes in the endoplasmic reticulum. Dissection of the enzyme into functional domains and studies by site-directed mutagenesis have enabled detailed characterization of the mechanism of electron transfer using stopped-flow and ...
Gutierrez, A, Grunau, A, Munro, AW, Roberts, GCK, Scrutton, NS, Paine, M, Wolf, CR   +6 more
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Crystallization of mitochondrial ubiquinol-cytochrome c reductase

Biochemistry, 1991
Ubiquinol-cytochrome c reductase of beef heart mitochondria was crystallized in the presence of decanoyl-N-methylglucamide, heptanetriol, and sodium chloride with poly(ethylene glycol) as precipitant. The largest crystal has dimensions of 4 x 2 x 1 mm. The crystalline enzyme is composed of 10 subunits.
W H, Yue, Y P, Zou, L, Yu, C A, Yu
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Microsomal cytochrome reductase

Biochimica et Biophysica Acta, 1957
P, STRITTMATTER, S F, VELICK
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Escherichia coli Cytochrome c Nitrite Reductase NrfA

2008
The periplasmic cytochrome c nitrite reductase (Nrf) system of Escherichia coli utilizes nitrite as a respiratory electron acceptor by reducing it to ammonium. Nitric oxide (NO) is a proposed intermediate in this six-electron reduction and NrfA can use exogenous NO as a substrate.
Clarke, Thomas A., Mills, Paul C., Poock, Susie R., Butt, Julea N., Cheesman, Myles R., Cole, Jeffrey A., Hinton, Jay C. D., Hemmings, Andrew M., Kemp, Gemma, Söderberg, Christopher A. G., Spiro, Stephen, van Wonderen, Jessica, Richardson, David J.   +12 more
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NADPH-Cytochrome P450 Reductase: Function

1993
In 1950, a report was published describing the isolation of a protein involved in the reduction of cytochrome c in animal tissue (Horecker 1950). The search for this enzyme was prompted by the previous discovery of an NADPH-cytochrome c reductase in yeast (Haas et al. 1940). The yeast enzyme was shown to use NADPH as the source of reducing equivalents,
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NADPH-Dependent Cytochrome P450 Reductase

1991
The pioneering studies of Horecker (1), Phillips and Langdon (2), Williams and Kamin (3) established that the microsomal NADPH-cytochrome c reductase is a flavoprotein capable of reducing various electron acceptors. Subsequent studies by other investigators (4–6) suggested an involvement of this reductase in microsomal hydroxylation since like ...
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[Methemoglobinemias. Cytochrome b5-reductase deficiency].

Eksperimentalna meditsina i morfologiia, 1994
In the paper are considered the basic mechanisms, leading to accumulation of methemoglobin in the red blood cells. The inherited methemoglobinaemia, due to enzymatic failure of cytochrome B5-reductase is considered.
D T, Thu, L, Damianova
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Nitrate reductase (cytochrome)

1994
D. Schomburg, M. Salzmann, D. Stephan
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[91] NADH-cytochrome b5 reductase

1967
Publisher Summary Cytochrome b 5 reductase is active with either cytochrome b 5 or any one of a number of artificial electron acceptors. The spectrophotometric assay methods therefore utilize the absorbance changes, which measure NADH oxidation or electron acceptor reduction.
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