Active sites of two orthologous cytochromes P450 2E1: differences revealed by spectroscopic methods.

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.

authors

Anzenbacherova E,Hudecek J,Murgida D,Hildebrandt P,Marchal S,Lange R,Anzenbacher P

doi

10.1016/j.bbrc.2005.08.063

subject

Has Abstract

pub_date

2005-12-09 00:00:00

pages

477-82

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01775-4

journal_volume

338

pub_type

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