Introduction of a CuA site into the blue copper protein amicyanin from Thiobacillus versutus.
The C-terminal loop of the blue copper protein amicyanin, which contains three of the four active site ligands, has been replaced with a CuA binding loop. The purple protein produced has visible and EPR spectra identical to those of a CuA centre. Recent evidence strongly suggests that the CuA centre of cytochrome c oxidase and the A centre of nitrous oxide reductase are similar and are both binuclear. It therefore follows that the purple amicyanin mutant created here also possesses a binuclear CuA centre.
Dennison
C
C
Leiden Institute of Chemistry, Gorlaeus Laboratories, The Netherlands.
Vijgenboom
E
E
de Vries
S
S
van der Oost
J
J
Canters
G W
GW
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010088:Oxidoreductases / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D013053:Spectrophotometry; D013855:Thiobacillus / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D008667:Metalloproteins; D011994:Recombinant Proteins; C017079:mauC protein, Methylobacterium extorquens; D003300:Copper; D010088:Oxidoreductases; C022763:nitrous oxide reductase; D003576:Electron Transport Complex IV