[Study of the iron-sulfur center N-2 from NADH-dehydrogenase in different metabolic states of the mitochondria from liver and heart].
The structural--equilibrium and nonequilibrium forms of the center N-2 from NADH-dehydrogenase differ in their parametres of the spin-lattice relaxation. The curves of the temperature dependence of the ESR signal intensity become the effective method of the study of the iron-sulphur proteins. The structural nonequilibrium form of the center N-2 was observed in the "4th" metabolic (by Chance) state, but equilibrium form of the center N-2 prevailed in the "3d" state or in the uncoupled state.
D000818:Animals; D002417:Cattle; D003579:Cytochrome Reductases / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D007700:Kinetics; D008667:Metalloproteins / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000378:metabolism*; D013696:Temperature
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase
Issledovanie zhelezosernogo tsentra N-2 NADN-degidrogenazy v razlichnykh metabolicheskikh sostoianiiakh mitokhondriĭ pecheni i serdtsa.