The binding of glutathione, some related molecules and two redox compounds to crystals of glutathione reductase has been investigated by X-ray crystallography at 0.3-nm resolution. Models for several bound ligands have been built and subjected to crystallographic refinement. The results clearly show the residues involved in glutathione binding as well as the geometry of the disulfide exchange. Glutathione-I is bound in a V-shaped conformation, while glutathione-II is extended. The zwitterionic glutamyl end of glutathione-II appears to be the most tightly bound part of the substrate. All glutathione conjugates and derivatives studied show binding dominated by the interactions at this site. In the reduced enzyme, glutathione-I forms a mixed d...
The FAD-binding site in dimeric glutathione reductase has been elucidated by application of sequence...
The human pi-class glutathione S-transferase (hGST P1-1) is a target for structure-based inhibitor d...
The conformation of the bound glutathione (GSH) in the active site of the human glutathione transfer...
The mode of binding of NADPH and oxidized glutathione to the flavoenzyme glutathione reductase has b...
The binding of the substrate NADPH as well as a number of fragments and derivatives of NADPH to glut...
An electron density map of the FAD-containing enzyme glutathione reductase from human erythrocytes w...
The activity of glutathione reductase with an unnatural analog of oxidized glutathione was explored....
Cytosolic GSTs (glutathione transferases) are a multifunctional group of enzymes widely distributed ...
Efficient enzyme catalysis depends on exquisite details of structure beyond those resolvable in typi...
Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omeg...
Glutathione reductase (Mr 2 x 52 500), a flavoenzyme of known three-dimensional structure, catalyses...
S-Conjugates of glutathione influence the glutathione/glutathione disulfide (GSH/GSSG) status of hep...
Three-dimensional structures of two redox enzymes, glutathione peroxidase from human plasma and a pr...
The C-terminal region in class Alpha glutathione transferase A1-1 (GSTA1-1), which forms an amphipat...
FAD-modified human glutathione reductases were reconstituted from apoenzyme using the FAD analogues ...
The FAD-binding site in dimeric glutathione reductase has been elucidated by application of sequence...
The human pi-class glutathione S-transferase (hGST P1-1) is a target for structure-based inhibitor d...
The conformation of the bound glutathione (GSH) in the active site of the human glutathione transfer...
The mode of binding of NADPH and oxidized glutathione to the flavoenzyme glutathione reductase has b...
The binding of the substrate NADPH as well as a number of fragments and derivatives of NADPH to glut...
An electron density map of the FAD-containing enzyme glutathione reductase from human erythrocytes w...
The activity of glutathione reductase with an unnatural analog of oxidized glutathione was explored....
Cytosolic GSTs (glutathione transferases) are a multifunctional group of enzymes widely distributed ...
Efficient enzyme catalysis depends on exquisite details of structure beyond those resolvable in typi...
Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omeg...
Glutathione reductase (Mr 2 x 52 500), a flavoenzyme of known three-dimensional structure, catalyses...
S-Conjugates of glutathione influence the glutathione/glutathione disulfide (GSH/GSSG) status of hep...
Three-dimensional structures of two redox enzymes, glutathione peroxidase from human plasma and a pr...
The C-terminal region in class Alpha glutathione transferase A1-1 (GSTA1-1), which forms an amphipat...
FAD-modified human glutathione reductases were reconstituted from apoenzyme using the FAD analogues ...
The FAD-binding site in dimeric glutathione reductase has been elucidated by application of sequence...
The human pi-class glutathione S-transferase (hGST P1-1) is a target for structure-based inhibitor d...
The conformation of the bound glutathione (GSH) in the active site of the human glutathione transfer...