E. Vakoufari et al., THE CRYSTAL-STRUCTURES OF REDUCED PSEUDOAZURIN FROM ALCALIGENES-FAECALIS-S-6 AT 2 PH VALUES, FEBS letters, 347(2-3), 1994, pp. 203-206
The structures of the reduced (Cu1+) blue-copper protein pseudoazurin
from Alcaligenes faecalis strain S-6 are refined at pH 7.8 and 4.4 usi
ng X-ray diffraction data to 1.8 Angstrom resolution. The final R-fact
ors for the high and low pH structures are 0.178 and 0.177, respective
ly. Comparing the reduced pseudoazurin at pH 7.8 with the oxidised (Cu
2+) molecule, small changes are observed in the vicinity of the copper
site and on the protein surface. At pH 4.4 the copper substituent imi
dazole of His(82) rotates away from the metal with a concurrent moveme
nt of the latter towards the plane of the remaining three ligands (Sy-
Cys(78), N delta 1-His(40) and S delta-Met(86)) thus the geometry of t
he copper site becomes planar trigonal.