In:
FEBS Letters, Wiley, Vol. 365, No. 1 ( 1995-05-22), p. 92-94
Abstract:
The C‐terminal loop of the blue copper protein amicyanin, which contains three of the four active site ligands, has been replaced with a Cu A binding loop. The purple protein produced has visible and EPR spectra identical to those of a Cu A centre. Recent evidence strongly suggests that the Cu A 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 Cu A centre.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(95)00429-D
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1460391-3
SSG:
12
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