Structural and kinetic studies on the activators of succinate dehydrogenase. 1977

L Susheela, and K Venkatesan, and T Ramasarma

1. Diverse classes of compounds such as dicarboxylates, pyrophosphates, quinols and nitrophenols are known to activate mitochondrial succinate dehydrogenase (EC 1.3.99.1). Examples in each class -- malonate, pyrophosphate, ubiquinol and 2,4-dinitrophenol -- are selected for comparative studies on the kinetic constants and structural relationship. 2. The activated forms of the enzyme obtained on preincubating mitochondria with the effectors exhibited Michaelian kinetics and gave double-reciprocal plots which are nearly parallel to that of the basal form. On activation, Km for the substrate also increased along with V. The effectors activated the enzyme at low concentrations and inhibited, in a competitive fashion, at high concentrations. The binding constant for activation was lower than that for inhibition for each effector. 3. These compounds possess ionizable twin oxygens separated by a distance of 5.5 +/- 0.8 A and having fractional charges in the range of -0.26 to -0.74 e. The common twin-oxygen feature of the substrate and the effectors suggested the presence of corresponding counter charges in the binding domain. The competitive nature of effectors with the substrate for inhibition further indicated the close structural resemblance of the activation and catalytic sites.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008314 Malonates Derivatives of malonic acid (the structural formula CH2(COOH)2), including its salts and esters.
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D011756 Diphosphates Inorganic salts of phosphoric acid that contain two phosphate groups. Diphosphate,Pyrophosphate Analog,Pyrophosphates,Pyrophosphate Analogs,Analog, Pyrophosphate
D004140 Dinitrophenols Organic compounds that contain two nitro groups attached to a phenol.
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D013385 Succinate Dehydrogenase A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II. Succinic Oxidase,Fumarate Reductase,Succinic Dehydrogenase,Dehydrogenase, Succinate,Dehydrogenase, Succinic,Oxidase, Succinic,Reductase, Fumarate
D014451 Ubiquinone A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals. Coenzyme Q

Related Publications

L Susheela, and K Venkatesan, and T Ramasarma
February 1997, Journal of enzyme inhibition,
L Susheela, and K Venkatesan, and T Ramasarma
January 1972, Physiological chemistry and physics,
L Susheela, and K Venkatesan, and T Ramasarma
September 1969, Biochimica et biophysica acta,
L Susheela, and K Venkatesan, and T Ramasarma
March 1972, European journal of biochemistry,
L Susheela, and K Venkatesan, and T Ramasarma
July 1977, Biochemistry,
L Susheela, and K Venkatesan, and T Ramasarma
July 1971, Biochimica et biophysica acta,
L Susheela, and K Venkatesan, and T Ramasarma
June 1970, European journal of biochemistry,
Copied contents to your clipboard!