title: Scanning tunneling microscopy study of cytochrome P450 2B4 incorporated in proteoliposomes.
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.
authors.affiliation: Laboratory of Physico-Chemical Methods of Analysis, Institute of Biomedical Chemistry, Moscow, Russia.
authors.lastname: Uvarov VYu
authors.forename: Y D
authors.initials: YD
authors.lastname: Ivanov
authors.forename: A N
authors.initials: AN
authors.lastname: Romanov
authors.forename: M O
authors.initials: MO
authors.lastname: Gallyamov
authors.forename: O I
authors.initials: OI
authors.lastname: Kiselyova
authors.forename: I V
authors.initials: IV
authors.lastname: Yaminsky
mesh_terms: D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism / Q000648:ultrastructure*; D006418:Heme; D016252:Microscopy, Scanning Tunneling; D011510:Proteolipids / Q000378:metabolism*; D051381:Rats; D013250:Steroid Hydroxylases / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D011510:Proteolipids; C020485:proteoliposomes; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C050356:steroid 15-alpha-hydroxylase