[The structural membrane control of the reduction of exogenous quinones catalysed by mitochondrial 2-methyl-1,4-naphthoquinone reductase].
The catalytic parameters of mitochondrial 2-methyl-1, 4-naphthoquinone-reductase were studied. Maximal velocity and Michaelis constant of quinone-reducing reaction were shown to depend strongly on the functional state of mitochondria (I, II and IV Chance's states). The changes in catalytic parameters were found for four quinone substrates essentially varying in their structures. For the same conditions the Michaelis constant of isolated enzyme remains unchanged. The data obtained indicate the possibility to control the activity and substrate specificity by structural rearrangements within the biological membrane.
D000818:Animals; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011808:Quinone Reductases / Q000378:metabolism*; D011809:Quinones / Q000378:metabolism*; D051381:Rats
D011809:Quinones; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases
Strukturno-membrannyĭ kontrol' vosstanovleniia ekzogennykh khinonov, kataliziruemogo mitokhondrial'noĭ 2-metil-1,4-naftokhinon-reduktazoĭ.