Oxidation of NAD dimers by horseradish peroxidase.

نویسندگان

  • L Avigliano
  • V Carelli
  • A Casini
  • A Finazzi-Agrò
  • F Liberatore
چکیده

Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both horseradish-peroxidase-catalysed oxidation and peroxidation of (NAD)2.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The peroxidase-dependent activation of butylated hydroxyanisole and butylated hydroxytoluene (BHT) to reactive intermediates. Formation of BHT-quinone methide via a chemical-chemical interaction.

The food antioxidants butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT) are shown to be metabolized to covalent binding intermediates and various other metabolites by prostaglandin H synthase and horseradish peroxidase. BHA was extensively metabolized by horseradish peroxidase (80% conversion of parent BHA into metabolites) resulting in the formation of three dimeric products. O...

متن کامل

Horseradish Peroxidase-catalyzed Two-electron Oxidations

The atypical two-electron oxidation of thioanisole and its p-methyl, p-methoxy, and p-nitro analogues by horseradish peroxidase, contrary to earlier reports, stereoselectively produces the (8) sulfoxides in 6070% enantiomeric excess. Horseradish peroxidase reconstituted with 6-meso-ethylheme has little peroxidase (guaiacol oxidizing) activity, as previously reported, but exhibits increased sulf...

متن کامل

Identification of acetaminophen polymerization products catalyzed by horseradish peroxidase.

Horseradish peroxidase catalyzed the H2O2-dependent oxidation and polymerization of acetaminophen. Six acetaminophen polymers were isolated from horseradish peroxidase reaction mixtures by semipreparative high pressure liquid chromatography. Chemical structures were determined by a combination of electron impact and chemical ionization mass spectrometry and 500-MHz proton magnetic resonance spe...

متن کامل

In Vitro Study of Acriflavine Interaction with Horseradish Peroxidase C

Acriflavine (3,6-diaminoacridine) is an anticeptic drug developed in 1912. Previous research has focused on investigation of the intercalating features of acriflavine, but little is known about its interaction with proteins. Drug-receptor interaction is of major interest in clinical science. The aim of the present study was to evaluate the ability of acriflavine to induce alterations in conform...

متن کامل

Characterization of dimers of hydroquinone glucosides produced by peroxidase-catalyzed polymerization.

4'-Hydroxyphenyl alpha-glucoside and 4'-hydroxyphenyl beta-glucoside were polymerized with horseradish peroxidase. The isolated dimers were found to have linkages at C3' of the hydroxyphenyl moieties and proved to be fluorescent. Low accumulation of oligomers was attributed to increasing electrochemical reactivity with polymerization degrees, which were expected from the levels of highest occup...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Biochemical journal

دوره 226 2  شماره 

صفحات  -

تاریخ انتشار 1985