Structural characterization of azurin from Pseudomonas aeruginosa and some of its methionine-121 mutants.
Azurin from Pseudomonas aeruginosa and two mutants where the methionine ligand has been mutated have been studied in order to directly investigate the functional and structural significance of this ligand in the blue copper proteins. Reduction potentials, X-ray absorption fine structure (XAFS), electron paramagnetic resonance (EPR), and optical spectra are obtained in an attempt to provide a direct correlation between the spectrochemical properties and the immediate structure of this redox center.
Molecular Biophysics Group, Daresbury Laboratory, Warrington, Cheshire, U.K.
L M
LM
Murphy
R W
RW
Strange
B G
BG
Karlsson
L G
LG
Lundberg
T
T
Pascher
B
B
Reinhammar
S S
SS
Hasnain
D015502:Absorptiometry, Photon; D000595:Amino Acid Sequence; D001400:Azurin / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001665:Binding Sites; D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000235:genetics; D005583:Fourier Analysis; D008715:Methionine; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D013053:Spectrophotometry
D001400:Azurin; D003300:Copper; D008715:Methionine