Copper(II) compound with long Cu(II)-phenolic oxygen atom bonding as galactose oxidase model

Sayo Ito, Satoshi Nishino, Hiroki Itoh, Shigeru Ohba, Yuzo Nishida

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Abstract

A crystal structure determination of Cu(phpyH)ClClO4 • CH3OH revealed that the protonated phenolic oxygen atom lies at the apex of a square pyramidal CuN4O arrangement with Cu(II) - O(phenolic) distances of 2.46 and 2.57 Å; this is a novel copper(II) model compound for galactose oxidase where the Cu(II)-phenolic oxygen (Tyrosine-495) distance is rather long, 2.69 Å, and the present results may provide chemical evidence for possible participation of Tyrosine-495 in the oxidation of galactose.

Original languageEnglish
Pages (from-to)1637-1642
Number of pages6
JournalPolyhedron
Volume17
Issue number10
Publication statusPublished - 1998

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Keywords

  • Galactose oxidase model
  • Long Cu(II)-phenol bond
  • Tyrosine residue

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry
  • Physical and Theoretical Chemistry
  • Materials Chemistry

Cite this

Ito, S., Nishino, S., Itoh, H., Ohba, S., & Nishida, Y. (1998). Copper(II) compound with long Cu(II)-phenolic oxygen atom bonding as galactose oxidase model. Polyhedron, 17(10), 1637-1642.