Determination of the Redox Properties of Human NADPH-Cytochrome P450 Reductase

Midpoint reduction potentials for the flavin cofactors in human NADPH-cytochrome P450 oxidoreductase were determined by anaerobic redox titration of the diflavin (FAD and FMN) enzyme and by separate titrations of its isolated FAD/NADPH and FMN domains. Flavin reduction potentials are similar in the...

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Veröffentlicht in:	Biochemistry (Easton) 2001-02, Vol.40 (7), p.1956-1963
Hauptverfasser:	Munro, Andrew W, Noble, Michael A, Robledo, Laura, Daff, Simon N, Chapman, Stephen K
Format:	Artikel
Sprache:	eng
Schlagworte:	Electron Transport Flavin Mononucleotide - analogs & derivatives Flavin Mononucleotide - chemistry Flavin Mononucleotide - metabolism Flavin-Adenine Dinucleotide - chemistry Flavin-Adenine Dinucleotide - metabolism Humans Isoenzymes - chemistry Isoenzymes - isolation & purification Isoenzymes - metabolism NADPH-Ferrihemoprotein Reductase - chemistry NADPH-Ferrihemoprotein Reductase - isolation & purification NADPH-Ferrihemoprotein Reductase - metabolism Oxidation-Reduction Potentiometry Protein Structure, Tertiary Reproducibility of Results Solubility
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