Tryptophan 83, a residue strongly involved in the intersubunit interaction of the Cu,Zn superoxide dismutases from Photobacterium leiognathi, has been selectively mutated to phenylalanine or tyrosine. The recombinant mutant enzymes expressed in Escherichia coil were purified in two well distinct and stable forms, one dimeric and fully active and the other monomeric and devoid of metals. In agreement, in vitro experiments indicate that the removal and addition of zinc in the mutant enzymes induces monomerization and dimerization, respectively, while does not perturb the dimeric association of the native protein. This is the first unambiguous experimental proof of a direct communication between the intersubunit interface and the metal active ...
AbstractWe have investigated the availability of zinc in the periplasmic space of Escherichia coli u...
AbstractThe equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase m...
A single mutation (Val29 --> Gly) at the subunit interface of a Cu, Zn superoxide dismutase dimer...
Tryptophan 83, a residue strongly involved in the intersubunit interaction of the Cu,Zn superoxide d...
The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,...
The influence of the constitutive metal ions on the equilibrium properties of dimeric Photobacterium...
The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,...
The Val28-->Gly single mutant at the subunit interface of Cu,Zn superoxide dismutase from Photoba...
Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that ...
AbstractThe Val28→Gly single mutant at the subunit interface of Cu,Zn superoxide dismutase from Phot...
To investigate the structural/functional role of the dimeric structure in Cu,Zn superoxide dismutase...
The bridging His63 residue in human Cu, Zn superoxide dismutase, which binds both metals, has been r...
To establish whether the species-specific variations at the subunit interface of bacterial Cu,Zn sup...
We have investigated the availability of zinc in the periplasmic space of Escherichia coli using a m...
AbstractWe have investigated the availability of zinc in the periplasmic space of Escherichia coli u...
AbstractThe equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase m...
A single mutation (Val29 --> Gly) at the subunit interface of a Cu, Zn superoxide dismutase dimer...
Tryptophan 83, a residue strongly involved in the intersubunit interaction of the Cu,Zn superoxide d...
The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,...
The influence of the constitutive metal ions on the equilibrium properties of dimeric Photobacterium...
The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,...
The Val28-->Gly single mutant at the subunit interface of Cu,Zn superoxide dismutase from Photoba...
Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that ...
AbstractThe Val28→Gly single mutant at the subunit interface of Cu,Zn superoxide dismutase from Phot...
To investigate the structural/functional role of the dimeric structure in Cu,Zn superoxide dismutase...
The bridging His63 residue in human Cu, Zn superoxide dismutase, which binds both metals, has been r...
To establish whether the species-specific variations at the subunit interface of bacterial Cu,Zn sup...
We have investigated the availability of zinc in the periplasmic space of Escherichia coli using a m...
AbstractWe have investigated the availability of zinc in the periplasmic space of Escherichia coli u...
AbstractThe equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase m...
A single mutation (Val29 --> Gly) at the subunit interface of a Cu, Zn superoxide dismutase dimer...