Identification of Histidine-60 Interaction with Copper in Activation of Chironomidae Ferrochelartase

Title: Identification of Histidine-60 Interaction with Copper in Activation of Chironomidae Ferrochelartase

Volume: 13 Issue: 5

Author(s): Kwong Fai Wong and John W. Ho

Affiliation:

Keywords: Ferrochelatase, mutagenesis, copper, catalytic mode, interaction

Abstract: 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.

Cite this article as:

Fai Wong Kwong and Ho W. John, Identification of Histidine-60 Interaction with Copper in Activation of Chironomidae Ferrochelartase, Protein & Peptide Letters 2006; 13 (5) . https://dx.doi.org/10.2174/092986606776819655

DOI https://dx.doi.org/10.2174/092986606776819655	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305