Kinetic and mechanistic studies on the reduction of melilotate hydroxylase by reduced pyridine nucleotides.
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چکیده
منابع مشابه
Kinetic and mechanistic studies on the oxidation of the melilotate hydroxylase . 2-OH-cinnamate complex by molecular oxygen.
The reaction mechanism of melilotate hydroxylase in the presence of 2-OH-cinnamate has been investigated by equilibrium titration, steady state kinetic and rapid reaction kinetic techniques. Analysis of the rapid reaction results for the reoxidation of reduced enzyme . 2-OH-cinnamate complex by molecular oxygen revealed the presence of an intermediate with visible absorption spectrum very simil...
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A soluble enzyme system which catalyzes the aerobic oxidation of reduced pyridine nucleotides in wheat germ has previously been described (1). Peroxidase was shown to be a component of this system. Later, Humphreys (2) demonstrated that Mn+ and an unidentified cofactor were required for aerobic oxidation of TPNH’ in crude preparations of malic enzyme from wheat germ. Although no attempt was mad...
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The reductions of either acyl or alkyl derivatives of dihydroxyacetone phosphate by enzymes from ascites tumor cell microsomes with NADPH were studied. The reaction rate was measured by determining the formation of labeled lipid from [4-3H]NADPH. The products were characterized as either 1-acyl or 1-alkyl [2-3H]glycerol d-phosphate formed from the corresponding keto derivatives. The enzymes wer...
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15 صفحه اولPlatinum-oxygen Bond Formation: Kinetic and Mechanistic Studies
Reaction of [PtMe(C^N)(SMe2)] (C^N = 2-phenylpyridinate (ppy); 1a, C^N = benzo[h]quinolate, (bhq); 1b) with hydrogen peroxide gives the platinum(IV) complexes trans-[PtMe(OH)2(C^N)(H2O)] (C^N = ppy; 3a, C^N = bhq, 3b) bearing platinum-oxygen bonds. The Pt(II) complexes 1a and 1b have 5dπ(Pt)→π*(C^N) MLCT band in the visible region which is used to easily follow the kinetic of its reaction with ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)86567-5