[Mechanism of enzymatic dismutation of superoxide anion-radicals].
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.
Kornienko
I V
IV
Central Forensic Identification Laboratory, Ministry of Defense of the Russian Federation, ul. Lermontovskaya 60, Rostov-na-Donu, 344010 Russia.
Kletskiĭ
M E
ME
Kornienko
I E
IE
Vnukov
V V
VV
Vodolazhskiĭ
D I
DI
D005609:Free Radicals / Q000737:chemistry; D008239:Lysine / Q000737:chemistry*; D011048:Polarography; D011789:Quantum Theory; D013482:Superoxide Dismutase / Q000737:chemistry*; D013816:Thermodynamics
D005609:Free Radicals; D013482:Superoxide Dismutase; D008239:Lysine