INTRODUCTION OF A CU-A SITE INTO THE BLUE COPPER PROTEIN AMICYANIN FROM THIOBACILLUS-VERSUTUS

The C-terminal loop of the blue copper protein amicyanin, which contai ns three of the four active site ligands, has been replaced with a Cu- A binding loop, The purple protein produced has visible and EPR spectr a identical to those of a Cu-A centre. Recent evidence strongly sugges ts that the Cu-A centre of cytochrome c oxidase and the A centre of ni trous 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.