Sumathi, S and Dasgupta, Dipak (2006) Interaction of 3-hydroxybenzoate-6-hydroxylase with cibacron blue. In: Journal of Enzyme Inhibition and Medicinal Chemistry, 21 (1). pp. 47-53.Full text not available from this repository.
Cibacron blue is a potent inhibitor of 3-HBA-6-hydroxylase at a concentration < 1 mu M. Kinetic analyses revealed that at a concentration below 0.5 mu M the dye behaves as an uncompetitive inhibitor with respect to 3-HBA and competes with NADH for the same site on the enzyme. The alteration of the near-UV CD spectrum and quenching of the emission fluorescence of the enzyme by cibacron blue indicates a significant alteration in the environment of aromatic amino acid residues due to a stacking interaction and subtle conformatiodnal changes in the enzyme. The concentration-dependent quenching of the intrinsic fluorescence of the enzyme by cibacron blue was employed to determine the binding parameters such as association constant (K-a) and stoichiometry (r) for the enzyme-dye complex.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Taylore and Francies.|
|Keywords:||cibacron blue; circular dichroism; competitive; flavin; fluorescence; 3-hydroxybenzoate; inhibition; uncompetitive; monooxygenase; 3-hydroxybenzoate-6-hydroxylase.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||17 Sep 2010 04:59|
|Last Modified:||17 Sep 2010 04:59|
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