Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution

Kensuke Nakamura, Takeshi Kawabata, Kei Yura, Nobuhiro Go

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.

Original languageEnglish
Pages (from-to)239-244
Number of pages6
JournalFEBS Letters
Volume553
Issue number3
DOIs
Publication statusPublished - 2003 Oct 23
Externally publishedYes

Keywords

  • Copper binding protein
  • Cupredoxin
  • Cyanobacterium
  • Genome sequence
  • Phylogeny
  • Rhizobium

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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