Scanning tunneling microscopy study of cytochrome P450 2B4 incorporated in proteoliposomes.
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.
Uvarov VYu
Laboratory of Physico-Chemical Methods of Analysis, Institute of Biomedical Chemistry, Moscow, Russia.
Ivanov
Y D
YD
Romanov
A N
AN
Gallyamov
M O
MO
Kiselyova
O I
OI
Yaminsky
I V
IV
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*
D011510:Proteolipids; C020485:proteoliposomes; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C050356:steroid 15-alpha-hydroxylase