Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin

S. I. Ozaki, M. P. Roach, T. Matsui, Y. Watanabe

研究成果: Article査読

136 被引用数 (Scopus)

抄録

To pursue structure - function relationships of heme enzymes in the activation of peroxides, we have chosen to use myoglobin as the framework for our molecular engineering studies. Comparison of the crystal structures of myoglobin and peroxidases reveals differences in the arrangement of amino acid residues in heme active sites. On the basis of these structural differences and the reaction mechanisms of peroxidases, we have converted myoglobin into a peroxidase-like enzyme by alternation of the heme distal pocket via site-directed mutagenesis. The replacement of the proximal histidine with cysteine and the exogenous substituted imidazoles slightly accelerates the peroxide O - O bond cleavage due to the electron donor characteristics. However, we have not observed an enhancement in the activation of peroxide by the proximal mutant with tyrosine, the exogenous phenolate, and benzoate. A clear understanding of the absolute role of the proximal ligand remains elusive.

本文言語English
ページ(範囲)818-825
ページ数8
ジャーナルAccounts of Chemical Research
34
10
DOI
出版ステータスPublished - 2001 11 7

ASJC Scopus subject areas

  • Chemistry(all)

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