Spectroelectrochemistry of blue copper proteins: pH and temperature dependences of the reduction potentials of five azurins

Cynthia Strong St. Clair, Walther R. Ellis, Harry B. Gray

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

Abstract

The pH and temperature dependences of the reduction potentials of Alcaligenes denitrificans (Ade), Pseudomonas aeruginosa (Pae), Alcaligenes faecalis (Afa), Alcaligenes sp. (Asp) and Bordetella bronchiseptica (Bbr) azurins have been determined by spectroelectrochemistry. Potentials at pH 8.0 (25 °C, μ 0.1 M, NaPi) are: 267.0 (Ade); 291.9 (Pae); 251.5 (Afa); 278.1 (Asp); 250.3 (Bbr) mV versus NHE. The variations in the potentials with pH are interpreted in terms of interactions between the copper site and titrating histidine residues. Variations in the reduction potential of Bbr azurin with both pH and temperature indicate that the copper site is distorted significantly by a redox-linked conformational change in this protein.

Original languageEnglish (US)
Pages (from-to)149-155
Number of pages7
JournalInorganica Chimica Acta
Volume191
Issue number1
DOIs
StatePublished - Jan 3 1992
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

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