Modi, Sandeep ; Behere, Digamber V. ; Mitra, Samaresh (1994) 1H- and 15N-NMR study of the binding of thiocyanate to chemically modified horseradish peroxidase and involvement of salt bridge Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1204 (1). pp. 14-18. ISSN 0167-4838
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...
Related URL: http://dx.doi.org/10.1016/0167-4838(94)90026-4
Abstract
The chemical modification of native horseradish peroxidase (HRP) has been carried out by esterification of the heme propionic group 15N- and 1H-NMR studies on binding of thiocyanate ion to chemically modified HRP have been utilized to demonstrate the existenceof salt bridge the heme propionic acid and distal amino acid group. The catalyzed oxidation of thiocyanate by the native HRP, and the chemically modified HRP has also been studied at different pH, and the significance of the salt bridge discussed.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | NMR, 1H-; NMR, 15N-;; Horseradish Peroxidase; Salt Bridge; Chemical Modification; Thiocyanate Binding |
| ID Code: | 20091 |
| Deposited On: | 20 Nov 2010 15:02 |
| Last Modified: | 03 Mar 2011 08:26 |
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