DOI | Trouver le DOI : https://doi.org/10.1016/S0891-5849(00)00298-7 |
---|
Auteur | Rechercher : Hodges, G.R.1; Rechercher : Young, M.J.1; Rechercher : Paul, T.1; Rechercher : Ingold, K. U.1 |
---|
Affiliation | - Conseil national de recherches du Canada
|
---|
Format | Texte, Article |
---|
Sujet | acetaldehyde; cytochrome c oxidase; hydrogen peroxide; superoxide; tetranitromethane; xanthine oxidase; chemical analysis; chemical reaction; competitive inhibition; electron transport; proton transport; reduction; acetaldehyde; comparative Study; cytochrome c; indicators and reagents; kinetics; milk; oxidation-reduction; spectrophotometry; superoxides; support, non-U.S. Gov't; tetranitromethane; xanthine oxidase |
---|
Résumé | The rate of formation of superoxide measured by its reduction of tetranitromethane (TNM) and by its reduction of ferric cytochrome c (Fe(III) cc) are in excellent agreement when the superoxide is generated from a simple chemical precursor. In contrast, the rate of formation of superoxide generated in the reaction of xanthine oxidase with acetaldehyde is much higher (up to a factor of 6) when measured with TNM and compared with Fe(III) cc. It is shown that Fe(III) cc measures superoxide that has diffused from the enzyme, and that TNM probably scavenges all the dioxygen that is reduced by one electron by the enzyme. The TNM traps enzyme-bound superoxide in competition with the second-electron transfer and proton transfer, which normally yield hydrogen peroxide. The proton transfer is probably rate determining, k(p) ≤ 3.8 x 103s-1. (C) 2000 Elsevier Science Inc. |
---|
Date de publication | 2000 |
---|
Dans | |
---|
Langue | anglais |
---|
Publications évaluées par des pairs | Oui |
---|
Numéro NPARC | 21276687 |
---|
Exporter la notice | Exporter en format RIS |
---|
Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
---|
Identificateur de l’enregistrement | 417cf1e6-505f-4c1d-91ad-5741dd5b8c07 |
---|
Enregistrement créé | 2015-10-13 |
---|
Enregistrement modifié | 2020-03-26 |
---|