Intramolecular electron transport in human ferroxidase (caeruloplasmin)

Author:

De Ley M1,Osaki S1

Affiliation:

1. Department of Chemistry, Florida State University, Tallahassee, Fla. 32306, U.S.A.

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 27 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Chloride Control of the Mechanism of Human Serum Ceruloplasmin (Cp) Catalysis;Journal of the American Chemical Society;2019-06-15

2. Ceruloplasmin;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15

3. Ceruloplasmin;Handbook of Metalloproteins;2006-04-15

4. Direct electron transfer between copper-containing proteins and electrodes;Biosensors and Bioelectronics;2005-06

5. Direct Electrochemistry of Proteins and Enzymes;Perspectives in Bioanalysis;2005

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