Identification of histidine-60 interaction with copper in activation of Chironomidae ferrochelatase.
Site-directed mutagenesis study of the conserved residue in ferrochelatase of chironomidae showed the binding interaction of copper with histidine-60. The activities of the variants increase by > 4-fold with H60N and 2 fold with H60D. The study identifies for the first time that the highly conserved H60 is a key molecular determinant in directing a catalytically competent mode of metal binding in the active site.
Wong
Kwong Fai
KF
Department of Biochemistry, The Chinese University of Hong Kong, Shatin, Hong Kong.
Ho
John W
JW
D000818:Animals; D002683:Chironomidae / Q000201:enzymology*; D003300:Copper / Q000378:metabolism*; D004789:Enzyme Activation; D005294:Ferrochelatase / Q000235:genetics / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism*; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation
D019476:Insect Proteins; D006639:Histidine; D003300:Copper; D005294:Ferrochelatase