Intramolecular electron transport in human ferroxidase (caeruloplasmin)
- 1 December 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 151 (3) , 561-566
- https://doi.org/10.1042/bj1510561
Abstract
The oxidation of reduced human ferroxidase by molecular O2 was studied in a stopped-flow spectrophotometer. It was shown that the two type 1 copper atoms behave differently in the absence of iron. The effect of iron on the kinetic parameters was investiagted. A working model for intramolecular electron transport in the enzyme is proposed.Keywords
This publication has 15 references indexed in Scilit:
- Binding of water to “Types I and II” Cu2+ in proteinsBiochemical and Biophysical Research Communications, 1974
- The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasminBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- The reaction of nitric oxide with ceruloplasminBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- A new intermediate in the reoxidation of reduced human ceruloplasminFEBS Letters, 1972
- The ascorbate oxidase activity of caeruloplasminBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Kinetic studies of ceruloplasmin-azide interactionFEBS Letters, 1971
- Substrate Activation and the Kinetics of FerroxidaseJournal of Biological Chemistry, 1970
- Role of iron in the oxidase activity of ceruloplasminBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- KINETIC STUDIES OF FERROUS ION OXIDATION WITH CRYSTALLINE HUMAN FERROXIDASE .2. RATE CONSTANTS AT VARIOUS STEPS AND FORMATION OF A POSSIBLE ENZYME-SUBSTRATE COMPLEX1967
- Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)Journal of Biological Chemistry, 1966