Mondal, Madhu Sudan ; Mitra, Samaresh (1996) Kinetic studies of the two-step reactions of H2O2 with manganese-reconstituted myoglobin Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1296 (2). pp. 174-180. 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(96)00068-4
Abstract
Kinetics and thermodynamics of the reaction of manganese-reconstituted myoglobin (MnMb) with hydrogen peroxide have been investigated by the stopped-flow kinetic technique. The results show evidence of two-step formation of peroxide compound in MnMb. Detailed kinetic investigation provides the complete reaction mechanism of the formation of the peroxide compound. It is observed that the formation of the peroxide compound involves an equilibrium binding step with MnMb and H2O2. The H2O2 bound complex of MnMb undergoes irreversible transformation to the peroxide compound, MnMb-I. The microscopic rate constants, involved during these elementary transformation reactions, have been determined. The detailed thermodynamic investigation of the elementary transformation enables us to construct their energy diagram.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Manganese-reconstituted Myoglobin; Myoglobin; Reaction Kinetics; Reaction Thermodynamics; Hydrogen Peroxide; (Horse Heart) |
| ID Code: | 20099 |
| Deposited On: | 20 Nov 2010 15:01 |
| Last Modified: | 03 Mar 2011 08:09 |
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