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

Kwong      Fai Wong; John   W.   Ho

doi:10.2174/092986606776819655

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.

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

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Protein & Peptide Letters

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.

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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