Scanning tunneling microscopy study of cytochrome P450 2B4 incorporated in proteoliposomes

Uvarov VYu; Y D Ivanov; A N Romanov; M O Gallyamov; O I Kiselyova; I V Yaminsky

doi:10.1016/s0300-9084(97)82536-9

Scanning tunneling microscopy study of cytochrome P450 2B4 incorporated in proteoliposomes

Biochimie. 1996;78(8-9):780-4. doi: 10.1016/s0300-9084(97)82536-9.

Authors

Uvarov VYu¹, Y D Ivanov, A N Romanov, M O Gallyamov, O I Kiselyova, I V Yaminsky

Affiliation

¹ Laboratory of Physico-Chemical Methods of Analysis, Institute of Biomedical Chemistry, Moscow, Russia.

PMID: 9010607
DOI: 10.1016/s0300-9084(97)82536-9

Abstract

In the present paper, the application of scanning tunneling microscopy in cytochrome P450s membrane topology is discussed. The method enables visualization of heme location in the lipid-bilayer-incorporated protein. It is supposed that the membrane-bound cytochrome P450 on the tunneling microscope substrate should behave as 'molecular diode'. A model explaining the liposome and the proteoliposome images observed is proposed.

MeSH terms

Animals
Aryl Hydrocarbon Hydroxylases*
Cytochrome P-450 Enzyme System / metabolism
Cytochrome P-450 Enzyme System / ultrastructure*
Heme
Microscopy, Scanning Tunneling
Proteolipids / metabolism*
Rats
Steroid Hydroxylases / metabolism
Steroid Hydroxylases / ultrastructure*

Substances

Proteolipids
proteoliposomes
Heme
Cytochrome P-450 Enzyme System
Steroid Hydroxylases
Aryl Hydrocarbon Hydroxylases
steroid 15-alpha-hydroxylase