Premium
Saturation kinetics of coenzyme Q in NADH and succinate oxidation in beef heart mitochondria
Author(s) -
Estornell E.,
Fato R.,
Castelluccio C.,
Cavazzoni M.,
Castelli G.Parenti,
Lenaz G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81378-y
Subject(s) - kinetics , mitochondrion , chemistry , saturation (graph theory) , cofactor , biochemistry , coenzyme q – cytochrome c reductase , enzyme kinetics , enzyme , mathematics , physics , cytochrome c , quantum mechanics , active site , combinatorics
The saturation kinetics of NADH and succinate oxidation for Coenzyme Q (CoQ) has been re‐investigated in pentane‐extracted lyophilized beef heart mitochondria reconstituted with exogenous CoQ 10 . The apparent ‘ K m ’ for CoQ 10 was one order of magnitude lower in succinate cytochrome c reductase than in NADH cytochrome c reductase. The K m value in NADH oxidation approaches the natural CoQ content of beef heart mitochondria, whereas that in succinate oxidation is close to the content of respiratory chain enzymes.