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. (Request a copy)Abstract
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 |
---|---|
Publication: | Journal of Enzyme Inhibition and Medicinal Chemistry |
Publisher: | Taylore and Francies |
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 |
URI: | http://eprints.iisc.ac.in/id/eprint/31729 |
Actions (login required)
View Item |