Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation
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Lorena G. Fenoll
, Francisco García-Molina , María A. Gilabert , Ramón Varón , Pedro A. García-Ruiz , José Tudela , Francisco García-Cánovas und José N. Rodríguez-López
Abstract
The catalytic cycle of heme peroxidases involves three processes: the formation of compound I, its conversion to compound II and regeneration of the native enzyme. Each of the processes consists of a reversible binding stage followed by an irreversible transformation stage. Our group has proposed a continuous, sensitive and reliable chronometric method for measuring the steady-state rate of peroxidase activity. Furthermore, we have derived an analytical expression for the steady-state rate and simplified it, taking into consideration the experimental values of the rate constants of some stages previously determined by other authors in stopped-flow assays. We determined the value of the constant for the transformation of a series of phenols and anilines by compound II, and found that it involves a deprotonation step and an electron transfer step. Study of the solvent deuterium isotope effect on the oxidation of phenol revealed the non-rate-limiting character of the deprotonation step in a proton inventory study. Usage of the Marcus equation showed that the electronic transfer step is rate-limiting in both cases, while phenols and anilines were oxidised at different rates for the same potentials. This can be attributed to the shorter electron-tunnelling distance for electron transfer to the iron ion in the phenols than in the anilines.
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Artikel in diesem Heft
- Supplementary material to the paper “The connexin gene family in mammals”
- Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
- The connexin gene family in mammals
- Hydrogen peroxide causes greater oxidation in cellular RNA than in DNA
- Homology modeling and SAR analysis of Schistosoma japonicum cathepsin D (SjCD) with statin inhibitors identify a unique active site steric barrier with potential for the design of specific inhibitors
- Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation
- P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro
- The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells
- Visualisation of transforming growth factor-β1, tissue kallikrein, and kinin and transforming growth factor-β receptors on human clear-cell renal carcinoma cells
- cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
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