Abstract
The rate constant for the hydride transfer step during oxidation of ethanol by cabroxymethylated alcohol dehydrogenase (alcohol:NAD + oxidoreductase, EC 1.1.1.1) is dependent on a group with p K a 7.5. This p K a is higher than that for the native enzyme. A mechanism is proposed to account for the ionisation and the protein fluorescence change which occur during formation of the carboxymethylated enzyme-NAD +-ethanol complex.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics
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