Structural changes on binding FAD and FAD-analogous and on site-directed 
mutagenesis of glutathione reductase

Schulz, Georg E.; Ermler, Ulrich

doi:10.1515/9783110855425-098

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Structural changes on binding FAD and FAD-analogous and on site-directed mutagenesis of glutathione reductase

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Schulz, G. E., & Ermler, U. (1991). Structural changes on binding FAD and FAD-analogous and on site-directed mutagenesis of glutathione reductase. In B. Curti (Ed.), Flavins and Flavoproteins 1990 (pp. 505-512). Berlin, New York: Walter de Gruyter. doi:10.1515/9783110855425-098.

Cite as: https://hdl.handle.net/21.11116/0000-0008-37ED-0

Abstract

Glutathione reductase from human erythrocytes was the first flavoenzyme studied in great structural detail. It belongs to a sizable family of flavoenzymes. Several binding studies were pursued at medium resolution. At high resolution 4 intermediate states were analyzed and refined, yielding a detailed view of the catalytic cycle. The apo-enzyme is rather stable and could be crystallized. It can be used for reconstituting the holo-enzyme with FAD and with a number of FAD-analogues. The changes after removal of FAD and after reconstitution with FAD-analogues are here discussed. Glutathione reductase from E.coli has been analyzed by site-directed mutagenesis as guided by the known homologous structure of the human enzyme (53% identity, Ref.26). Most conspicuous was the change from NADPH to NADH by seven individual point mutations. For analyzing these mutants in detail we solved the structure of the E.coli enzyme.