The photoreactivity of the copper-NO complexes in cytochrome c oxidase and in other copper-containing proteins.

Autor: Wever R, Boelens R, De Boer E, Van Gelder BF, Gorren AC, Rademaker H
Jazyk: angličtina
Zdroj: Journal of inorganic biochemistry [J Inorg Biochem] 1985 Mar-Apr; Vol. 23 (3-4), pp. 227-32.
DOI: 10.1016/0162-0134(85)85029-7
Abstrakt: The complexes of NO with CuB of cytochrome c oxidase in which cytochrome a3 may or may not be ligated to cyanide or fluoride are photodissociable. NO does not appear to react with CuB in complexes of cytochrome c oxidase in which sulphide or mercaptans are ligated to the haem iron of cytochrome a3. A comparison is made between the photoreactivity of the complexes of NO with cytochrome c oxidase and those with ceruloplasmin, ascorbate oxidase, and haemocyanin. It is shown that the photoreactivity of CuB 2+.NO in cytochrome c oxidase is not unique for this enzyme, but may also be observed in the complexes of NO with type-1 copper-containing enzymes. This would suggest that the ligation of CuB in cytochrome c oxidase shows some similarity to type-1 copper in blue oxidases.
Databáze: MEDLINE