Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa.

doi:10.1016/0167-4838(95)00059-4

Back to search

Article

Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa.

Biochimica et biophysica acta - 16 Aug 1995

Bonander N, Karlsson B G, Vänngård T

Abstract excerpt

In the family of small blue-copper proteins azurins are unique in that they contain a disulfide bridge close to the amino-terminal end. It is situated in the 'south' side of the molecule, about 25 A away from the copper. Site-specific mutagenesis was used to exchange one or both of the cysteines...

Topics

Azurin
Circular Dichroism
Copper
Cysteine
Disulfides
Electron Spin Resonance Spectroscopy
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Pseudomonas aeruginosa
Serine
Spectrometry, Fluorescence
Spectrophotometry

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.