The photoreactivity of the copper-NO complexes in cytochrome c oxidase and in other copper-containing proteins.
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.
Wever
R
R
Boelens
R
R
De Boer
E
E
Van Gelder
B F
BF
Gorren
A C
AC
Rademaker
H
H
D000818:Animals; D001204:Ascorbate Oxidase / Q000378:metabolism; D002417:Cattle; D002570:Ceruloplasmin / Q000378:metabolism; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000378:metabolism* / Q000528:radiation effects; D006433:Hemocyanins / Q000378:metabolism; D008027:Light; D009206:Myocardium / Q000201:enzymology; D009569:Nitric Oxide / Q000378:metabolism*; D010777:Photochemistry
D009569:Nitric Oxide; D003300:Copper; D006433:Hemocyanins; D001204:Ascorbate Oxidase; D002570:Ceruloplasmin; D003576:Electron Transport Complex IV