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The Active Site of Glutathione Reductase: An Example of Near Transition‐State Structures
Author(s) -
Sustmann Refiner,
Sicking Willi,
Schulz Georg E.
Publication year - 1989
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198910231
Subject(s) - active site , hydride , mndo , glutathione reductase , nucleophile , glutathione , chemistry , parametrization (atmospheric modeling) , stereochemistry , interpretation (philosophy) , disulfide bond , computational chemistry , physics , biochemistry , molecule , enzyme , metal , organic chemistry , quantum mechanics , computer science , catalysis , glutathione peroxidase , radiative transfer , programming language
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.