title: The photoreactivity of the copper-NO complexes in cytochrome c oxidase and in other copper-containing proteins.
abstract: 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.
authors.forename: R
authors.initials: R
authors.lastname: Wever
authors.forename: R
authors.initials: R
authors.lastname: Boelens
authors.forename: E
authors.initials: E
authors.lastname: De Boer
authors.forename: B F
authors.initials: BF
authors.lastname: Van Gelder
authors.forename: A C
authors.initials: AC
authors.lastname: Gorren
authors.forename: H
authors.initials: H
authors.lastname: Rademaker
mesh_terms: 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
chemical_list: D009569:Nitric Oxide; D003300:Copper; D006433:Hemocyanins; D001204:Ascorbate Oxidase; D002570:Ceruloplasmin; D003576:Electron Transport Complex IV