Flexibility and stability of the structure of cytochromes P450 3A4 and BM‐3

The flexibility of the structure and compressibility of the respective active site of cytochromes P450 3A4 (CYP3A4) and BM‐3 (CYP102) were studied using absorption spectroscopy in the ultraviolet and visual regions. Conformational changes in the overall protein structures of both CYP3A4 and CYP102 d...

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Veröffentlicht in:	European journal of biochemistry 2000-05, Vol.267 (10), p.2916-2920
Hauptverfasser:	Anzenbacherová, Eva, Bec, Nicole, Anzenbacher, Pavel, Hudeček, Jiří, Souček, Pavel, Jung, Christiane, Munro, Andrew W., Lange, Reinhard
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins Binding Sites Carbon Monoxide - chemistry compressibility conformation CYP102 CYP3A4 Cytochrome P-450 CYP3A Cytochrome P-450 Enzyme System - chemistry derivative spectra Enzyme Stability Escherichia coli - enzymology Heme - chemistry Mixed Function Oxygenases - chemistry NADPH-Ferrihemoprotein Reductase Plasmids Pliability Pressure Protein Binding Protein Conformation Spectrophotometry Temperature Troleandomycin - chemistry
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