Evidence from the acceleration of cytochromecreduction for the formation of ascorbate free radical by dopamine β-monooxygenase
- 1 December 1979
- journal article
- Published by Wiley in FEBS Letters
- Vol. 108 (1) , 25-27
- https://doi.org/10.1016/0014-5793(79)81170-9
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- On the amphiphilic and hydrophilic forms of dopamine β‐mono‐oxygenase in bovine adrenal medullaJournal of Neurochemistry, 1979
- The Enzyme‐Bound Copper of Dopamine β‐MonooxygenaseEuropean Journal of Biochemistry, 1979
- Dopamine β‐monooxygenase: electron paramagnetic resonance and oxidation‐reduction properties of the enzyme‐bound copperFEBS Letters, 1978
- A study of the molar absorptivity of ascorbic acid at different wavelengths and pH valuesAnalytica Chimica Acta, 1977
- Purification and Characterization of Dopamine β ‐Hydroxylase from Bovine Adrenal MedullaEuropean Journal of Biochemistry, 1976
- Dophamine β‐Hhydroxylase: Evidence against a ping‐pong mechanismFEBS Letters, 1974
- Magnetic resonance studies on the mechanism of the enzymic β-hydroxylation of 3,4-dihydroxyphenylethylamineBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
- Studies on the Peroxidase Effect of Cytochrome c. II. Purification of Beef Heart Cytochrome c by Gel Filtration.Acta Chemica Scandinavica, 1964
- Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactionsBiochimica et Biophysica Acta, 1961
- Identification by electron spin resonance spectroscopy of the primary product of tyrosinase-catalyzed catechol oxidationBiochemical and Biophysical Research Communications, 1961