title: [ESR-spectroscopy of cytochrome P-450 LM2 in the soluble and membrane-bound state].
abstract: Influence of microenvironment on the structure of spin-labeled cytochrome P-450 LM2 was studied. The distance between the spin-label which is covalently bound to cysteine-152 and heme ferrum in soluble protein is 17 A and 23 A in the membrane-bound one. The spin-label was exposed in water solution in both cases. It was shown that solubilized cytochrome P-450 LM2 in water solution forms the aggregates consisting of 4-6 monomers.
authors.forename: V Iu
authors.initials: VIu
authors.lastname: Uvarov
authors.forename: R M
authors.initials: RM
authors.lastname: Davydov
authors.forename: V P
authors.initials: VP
authors.lastname: Timofeev
mesh_terms: D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D004578:Electron Spin Resonance Spectroscopy; D008081:Liposomes / Q000032:analysis*; D008563:Membrane Lipids / Q000032:analysis*; D011487:Protein Conformation; D012995:Solubility
chemical_list: D008081:Liposomes; D008563:Membrane Lipids; D003577:Cytochrome P-450 Enzyme System
vernacular_title: EPR-spektroskopiia spin-mechenogo tsitokhroma P-450 LM2 v izolirovannom i membranno-sviazannom sostoianiiakh.