The inhibition of caeruloplasmin by cyanide

Autor:	B E, Speyer, G, Curzon
Rok vydání:	1968
Předmět:	Azides Kinetics History Cyanides Time Factors Spectrophotometry Methods Ceruloplasmin Articles Copper Protein Binding Computer Science Applications Education
Zdroj:	Biochemical Journal. 106:905-911
ISSN:	0306-3283
DOI:	10.1042/bj1060905
Popis:	1. The reversible inhibition of the oxidase activity of caeruloplasmin by cyanide was investigated. 2. The kinetics are unusual, being competitive but with the inhibited complex formed only during cycling. 3. Inhibitory concentrations of cyanide are comparable with that of caeruloplasmin. 4. One azide group completely inhibits a caeruloplasmin molecule but two cyanide groups are required. 5. The results suggest that azide binds to a half-reduced or fully reduced conformational isomer of the enzyme whereas cyanide binds to completely reoxidized isomers, and that inhibited complexes contain ligand bridges between copper atoms.
Databáze:	OpenAIRE
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