title: [Mechanism of enzymatic dismutation of superoxide anion-radicals].
abstract: The mechanism of interaction of the superoxide radical O2-. with lysine was studied by the methods of polarography and ab initio quantum chemical calculations. It was shown that O2-. interacts with lysine to form a thermodynamically stable complex with proton transfer and formation of the HO2. radical.
authors.affiliation: Central Forensic Identification Laboratory, Ministry of Defense of the Russian Federation, ul. Lermontovskaya 60, Rostov-na-Donu, 344010 Russia.
authors.forename: I V
authors.initials: IV
authors.lastname: Kornienko
authors.forename: M E
authors.initials: ME
authors.lastname: Kletskiĭ
authors.forename: I E
authors.initials: IE
authors.lastname: Kornienko
authors.forename: V V
authors.initials: VV
authors.lastname: Vnukov
authors.forename: D I
authors.initials: DI
authors.lastname: Vodolazhskiĭ
mesh_terms: D005609:Free Radicals / Q000737:chemistry; D008239:Lysine / Q000737:chemistry*; D011048:Polarography; D011789:Quantum Theory; D013482:Superoxide Dismutase / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D005609:Free Radicals; D013482:Superoxide Dismutase; D008239:Lysine