Sep 10, 1976

Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes

The Journal of Biological Chemistry
A S Abramovitz, V Massey

Abstract

Evidence is presented that the changes in absorption spectrum obtained on complex formation between Old Yellow Enzyme and phenolic compounds are due to charge-transfer interactions. The positive correlation between the energy of the long wavelength transition and the Hammett para constant with a series of para-substituted phenols indicates that the phenol is the charge-transfer donor and the oxidized flavin of the enzyme is the charge-transfer acceptor. The same conclusion is drawn from studies in which the flavin of the native enzyme, flavin mononucleotide, was replaced by a variety of artificial flavins of different oxidation-reduction potential. The effect of pH on the dissociation constant for the enzyme-ligand binding also indicates that it is the phenolate anion, rather than the conjugate acid, which is responsible for the charge-transfer interaction. The significance of these results is discussed relative to long wavelength absorbing species detected with other flavoproteins.

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Mentioned in this Paper

Energy Transfer
Structure-Activity Relationship
Plasma Protein Binding Capacity
Protein Conformation
Spectrophotometry, Ultraviolet
Phenols
Spectrophotometry
NADH, NADPH Oxidoreductases
Flavins
Saccharomyces cerevisiae

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