Abstract
Abstract EPR spectroscopy of a mixture of ethanolamine deaminase, 5′-deoxy-adenosylcobalamin and deuterated ethanolamine frozen during the act of catalysis revealed the appearance of a signal at g = 2.09. This signal disappeared when the reaction was permitted to continue until the substrate was exhausted, but reappeared upon subsequent addition of substrate. No signal was observed when enzyme or coenzyme was omitted from the reaction mixture, but small signals did appear when substrate was omitted. There were significant differences between these latter signals and the signal obtained from a sample containing all three components. This evidence is consistent with the hypothesis that species with unpaired electrons are involved in the mechanism of action of ethanolamine deaminase.
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