Rapid Conformational Dynamics of Cytochrome P450 2E1 in a Natural Biological Membrane Environment

• Published in: Biochemistry (Easton) Vol. 45; no. 51; pp. 15617 - 15623
• Main Authors: Smith, Stanley V, Robinson, Richard C, Smith, Tina G, Burks, Stephanie M, Friedman, Fred K
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 26.12.2006
• Subjects: Animals; Baculoviridae - enzymology; Baculoviridae - genetics; Binding Sites - genetics; Carbon Monoxide - chemistry; Carbon Monoxide - metabolism; Cytochrome P-450 CYP2E1 - chemistry; Cytochrome P-450 CYP2E1 - deficiency; Cytochrome P-450 CYP2E1 - genetics; Cytochrome P-450 CYP2E1 - metabolism; Genetic Vectors; Humans; Intracellular Membranes - enzymology; Intracellular Membranes - metabolism; Isoenzymes - chemistry; Isoenzymes - deficiency; Isoenzymes - genetics; Isoenzymes - metabolism; Kinetics; Mice; Mice, Inbred C57BL; Mice, Knockout; Microsomes, Liver - enzymology; Microsomes, Liver - metabolism; Protein Binding - genetics; Protein Conformation; Substrate Specificity - genetics

Among the members of the cytochrome P450 superfamily, P450 2E1 is most often associated with the production of reactive oxygen species and subsequent cellular toxicity. We sought to identify a structural basis for this distinguishing feature of P450 2E1 by examining its carbon monoxide binding kinet...