A micellar model for investigating the chemical nature of hydrogen transfer in NAD(P)H-dependent enzymatic reactions

Aqueous micelles of Triton X-100 were shown to catalyse the redox reaction between NADH and 2-p-iodophenyl-3-p-nitrophenyl-5-phenyltetrazolium chloride (INT) at the neutral pH. The transfer of reducing equivalents between the reactants in the micellar system appeared to be direct and quantitative. N...

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Veröffentlicht in:Biochemical and biophysical research communications 1989-03, Vol.159 (3), p.1330-1336
1. Verfasser: Rao, U.Mallikarjuna
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description Aqueous micelles of Triton X-100 were shown to catalyse the redox reaction between NADH and 2-p-iodophenyl-3-p-nitrophenyl-5-phenyltetrazolium chloride (INT) at the neutral pH. The transfer of reducing equivalents between the reactants in the micellar system appeared to be direct and quantitative. N-tert-butylphenyl-α-nitrone, a lipophilic free-radical scavenger which can enter micelles, and superoxide dismutase did not alter the stoichiometry of the reaction. The oxidation product of NADH was found to be 100% enzymatically active. The IR spectrum of INT-formazan (i.e., the product of INT reduction) showed an absorbance at 3,100–3,700 cm − due to NH-stretching. The presence of NH proton, confirmed further by IH-NMR, together with the above observations suggests that INT, as part of the over-all redox process, abstracts a C(4) hydrogen of the dihydropyridine nucleus of NADH with a simultaneous cleavage at N(2–3) position of its 1,2,3,4-tetrazole ring system and that the redox events are confined to a microenvironment as in the case of NAD(P)H-dependent enzymatic reactions.
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The transfer of reducing equivalents between the reactants in the micellar system appeared to be direct and quantitative. N-tert-butylphenyl-α-nitrone, a lipophilic free-radical scavenger which can enter micelles, and superoxide dismutase did not alter the stoichiometry of the reaction. The oxidation product of NADH was found to be 100% enzymatically active. The IR spectrum of INT-formazan (i.e., the product of INT reduction) showed an absorbance at 3,100–3,700 cm − due to NH-stretching. 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The transfer of reducing equivalents between the reactants in the micellar system appeared to be direct and quantitative. N-tert-butylphenyl-α-nitrone, a lipophilic free-radical scavenger which can enter micelles, and superoxide dismutase did not alter the stoichiometry of the reaction. The oxidation product of NADH was found to be 100% enzymatically active. The IR spectrum of INT-formazan (i.e., the product of INT reduction) showed an absorbance at 3,100–3,700 cm − due to NH-stretching. The presence of NH proton, confirmed further by IH-NMR, together with the above observations suggests that INT, as part of the over-all redox process, abstracts a C(4) hydrogen of the dihydropyridine nucleus of NADH with a simultaneous cleavage at N(2–3) position of its 1,2,3,4-tetrazole ring system and that the redox events are confined to a microenvironment as in the case of NAD(P)H-dependent enzymatic reactions.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2930563</pmid><doi>10.1016/0006-291X(89)92256-0</doi><tpages>7</tpages></addata></record>
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subjects Analytical, structural and metabolic biochemistry
Biological and medical sciences
Colloids
Detergents
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrogen
Kinetics
Micelles
Models, Theoretical
NAD - metabolism
NADH, NADPH Oxidoreductases - metabolism
NADP - metabolism
Octoxynol
Oxidation-Reduction
Oxidoreductases
Polyethylene Glycols
title A micellar model for investigating the chemical nature of hydrogen transfer in NAD(P)H-dependent enzymatic reactions
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