Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly.

doi:10.1021/bi951604w

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Article

Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly.

Biochemistry - 6 Feb 1996

van Pouderoyen G, Andrew C R, Loehr T M, Sanders-Loehr J, Mazumdar S, Hill H A, Canters G W

Abstract excerpt

The spectroscopic and mechanistic properties of the Cu-containing active site of azurin from Pseudomonas aeruginosa were investigated by the construction of a mutant in which one of the ligands of the metal, His46, was replaced by a glycine. Although the mutation creates a hole in the interior of...

Topics

Azurin
Copper
Electrochemistry
Ligands
Mutation
Protein Conformation
Pseudomonas aeruginosa
Recombinant Proteins
Spectrum Analysis

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