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

doi:10.1016/S0020-1693(00)80341-2

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

Biomedical Engineering

Research output: Contribution to journal › Article › peer-review

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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, NaP_i) 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 language	English (US)
Pages (from-to)	149-155
Number of pages	7
Journal	Inorganica Chimica Acta
Volume	191
Issue number	1
DOIs	https://doi.org/10.1016/S0020-1693(00)80341-2
State	Published - Jan 3 1992

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry
Materials Chemistry

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10.1016/S0020-1693(00)80341-2

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title = "Spectroelectrochemistry of blue copper proteins: pH and temperature dependences of the reduction potentials of five azurins",

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.",

author = "{St. Clair}, {Cynthia Strong} and Ellis, {Walther R.} and Gray, {Harry B.}",

note = "Funding Information: We thank Ellie Adman, Rich Bersohn, Angelo DiBilio, Brad Jacobs and Bo Malmstrom for helpful discussions.T his work was supportedb y NIH Grant DK19038 (contribution 8232 from the Arthur Amos Noyes Laboratory).",

year = "1992",

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doi = "10.1016/S0020-1693(00)80341-2",

language = "English (US)",

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T2 - pH and temperature dependences of the reduction potentials of five azurins

AU - St. Clair, Cynthia Strong

AU - Ellis, Walther R.

AU - Gray, Harry B.

N1 - Funding Information: We thank Ellie Adman, Rich Bersohn, Angelo DiBilio, Brad Jacobs and Bo Malmstrom for helpful discussions.T his work was supportedb y NIH Grant DK19038 (contribution 8232 from the Arthur Amos Noyes Laboratory).

PY - 1992/1/3

Y1 - 1992/1/3

N2 - 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.

AB - 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.

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

Abstract

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