Abstract:
:Cytochromes 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 as 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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Anzenbacherova E,Hudecek J,Murgida D,Hildebrandt P,Marchal S,Lange R,Anzenbacher Pdoi
10.1016/j.bbrc.2005.08.063subject
Has Abstractpub_date
2005-12-09 00:00:00pages
477-82issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)01775-4journal_volume
338pub_type
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