The Active Site of Glutathione Reductase: An Example of Near Transition‐State Structures
- 1 August 1989
- journal article
- research article
- Published by Wiley in Angewandte Chemie-International Edition
- Vol. 28 (8), 1023-1025
- https://doi.org/10.1002/anie.198910231
Abstract
Interactions in the active site of glutathione reductase were calculated at the MNDO level (PM3 parametrization). The reaction partners were found to be arranged in an ideal geometry for hydride transfer from NADPH to FAD and for nucleophilic opening of the protein disulfide bridge by FADH⊖. The X-ray structure analysis alone would have been insufficient for such an interpretation.Keywords
This publication has 11 references indexed in Scilit:
- A crystallographic study of the glutathione binding site of glutathione reductase at 0.3‐nm resolutionEuropean Journal of Biochemistry, 1989
- The transition state of the Diels-Alder reaction of butadiene and ethylene. A perturbational evaluation.Tetrahedron Letters, 1988
- Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductaseBiochemistry, 1988
- PMO Analysis of Cycloadditions, I Diels‐Alder Reactions of 2,3‐Bis(methylene)norbornaneEuropean Journal of Inorganic Chemistry, 1987
- Refined structure of glutathione reductase at 1.54 Å resolutionJournal of Molecular Biology, 1987
- Transition structures for hydride transfersJournal of the American Chemical Society, 1987
- Mechanism and transition-state structure of hydride-transfer reactions mediated by nad(p)h-modelsTetrahedron, 1986
- The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.Journal of Biological Chemistry, 1983
- Flavin coenzymes: at the crossroads of biological redox chemistryAccounts of Chemical Research, 1980
- 3 Flavin-Containing DehydrogenasesPublished by Elsevier BV ,1976