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Active sites of two orthologous cytochromes P450 2E1: Differences revealed by spectroscopic methods
Citation key ISI:000233296700068
Author Anzenbacherova, E and Hudecek, J and Murgida, D and Hildebrandt, P and Marchal, S and Lange, R and Anzenbacher, P
Pages 477-482
Year 2005
ISSN 0006-291X
DOI 10.1016/j.bbrc.2005.08.063
Address 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
Journal Biochem. Biophys. Res. Commun.
Volume 338
Number 1
Month DEC 9
Abstract Cytochronies P450 2E1 of human and minipig origin were examined by absorption spectroscopy under high hydrostatic pressure and by resonance Raman spectroscopy. Human enzyme tends to denature to the P420 form more easily than the minipig form moreover, the apparent compressibility of the heme active site (as judged from a redshift of the absorption maximum with pressure) is greater than that of the minipig counterpart. Relative compactness of the minipig enzyme is also seen in the Raman spectra, where the presence of planar heme conformation was inferred from band positions characteristic of the low-spin heme with high degree of symmetry. In this respect, the CYP2E1 seems to be another example of P450 conformational heterogeneity Lis shown, e.g., by Davydov et al. for CYP3A4 [Biochem. Biophys. Res. Commun. 312 (2003) 121-130]. The results indicate that the flexibility of the CYP active site is likely one of its basic structural characteristics. (c) 2005 Elsevier Inc. All rights reserved.
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