Outer Sphere Mutations Perturb Metal Reactivity in Manganese Superoxide Dismutase

Tyrosine 34 and glutamine 146 are highly conserved outer sphere residues in the mononuclear manganese active site of Escherichia coli manganese superoxide dismutase. Biochemical and spectroscopic characterization of site-directed mutants has allowed functional characterization of these residues in t...

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Veröffentlicht in:	Biochemistry (Easton) 2001-01, Vol.40 (1), p.15-27
Hauptverfasser:	Edwards, Ross A, Whittaker, Mei M, Whittaker, James W, Baker, Edward N, Jameson, Geoffrey B
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites - genetics Catalysis Circular Dichroism Computer Simulation Conserved Sequence Enzyme Activation - genetics Escherichia coli Escherichia coli - enzymology Glutamine - genetics Histidine - genetics Manganese - chemistry manganese superoxide dismutase Models, Molecular Mutagenesis, Site-Directed Phenylalanine - genetics Pyrobaculum aerophilum Spectrophotometry, Ultraviolet Superoxide Dismutase - chemistry Tyrosine - genetics
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