✦ LIBER ✦

Electronic, steric and lipophilicity requirements in the oxidation of dialkylarylamines by horseradish peroxidase

✍ Scribed by Guido Galliani; Bruno Rindone

Publisher: Elsevier Science
Year: 1980
Tongue: English
Weight: 184 KB
Volume: 40
Category: Article
ISSN: 0020-1693
DOI: 10.1016/s0020-1693(00)92236-9

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Electronic factors and lipophilicity in

Electronic factors and lipophilicity in the horseradish peroxidase-catalyzed oxidation of N, N-dialkylanilines with hydrogen peroxide and oxygen

✍ Guido Galliani; Bruno Rindone 📂 Article 📅 1981 🏛 Elsevier Science 🌐 English ⚖ 422 KB

Oxidation of spruce lignin by fungal lig

Oxidation of spruce lignin by fungal lignin peroxidase and horseradish peroxidase: Comparison of their actions on molecular structure of the polymer in colloidal solution

✍ Bernard Kurek; Bernard Monties 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 519 KB

Nitration Reaction Catalyzed by Horserad

Nitration Reaction Catalyzed by Horseradish Peroxidase in the Presence of H2O2 and NaNO2

✍ Rong-Ji DAI; Hui HUANG; Jie CHEN; Yu-Lin DENG; Sheng-Yuan XIAO 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 113 KB

## Abstract The enzymatic nitration of phenol and __m__‐cresol catalyzed by horseradish peroxidase was studied in the presence of H~2~O~2~ and NaNO~2~. The results showed that the nitration products of phenol were 2‐nitro and 4‐nitrophenols. There was also a small amount of by‐products of hydroquin

Steric and electronic effects on the oxi

Steric and electronic effects on the oxidation of ortho-substituted benzhydrols by chromic acid

✍ D.G. Lee; M. Raptis 📂 Article 📅 1973 🏛 Elsevier Science 🌐 French ⚖ 483 KB

A study has been made of the oxidation of a number of substituted benzhydrols by chromic acid in aqueous acetic acid. The reaction rate constants are linearly proportional to the KR+ values of the alcohols. ortho-Substitution increases the rate of reaction and reduces the magnitude of the primary ki

Oxidation of 4-bromophenol by the recomb

Oxidation of 4-bromophenol by the recombinant fused protein cellulose-binding domain-horseradish peroxidase immobilized on cellulose

✍ Ilan Levy; Gary Ward; Yitzhak Hadar; Oded Shoseyov; Carlos G. Dosoretz 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 230 KB

Enhanced chemiluminescence reaction appl

Enhanced chemiluminescence reaction applied to the study of horseradish peroxidase stability in the course ofp-iodophenol oxidation

✍ Kapeluich, Yuri L. ;Rubtsova, Maya Yu. ;Egorov, Alexey M. 📂 Article 📅 1997 🏛 John Wiley and Sons ⚖ 124 KB 👁 2 views

The enhanced chemiluminescence reaction (ECL) was applied to the study of horseradish peroxidase (HRP) inactivation during the oxidation of p-iodophenol. Enzyme inactivation was shown to be the main reason for light decay in the course of the reaction. No individual effect of luminol and p-iodopheno