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The structure of the flavoenzyme glutathione reductase

MPS-Authors
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Schulz,  G. E.
Max Planck Institute for Medical Research, Max Planck Society;

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Schirmer,  R. Heiner
Max Planck Institute for Medical Research, Max Planck Society;

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Sachsenheimer,  W.
Max Planck Institute for Medical Research, Max Planck Society;

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Pai,  Emil F.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Schulz, G. E., Schirmer, R. H., Sachsenheimer, W., & Pai, E. F. (1978). The structure of the flavoenzyme glutathione reductase. Nature, 273(5658), 120-124. doi:10.1038/273120a0.


Cite as: https://hdl.handle.net/21.11116/0000-0003-2375-2
Abstract
The three-dimensional structure of the dimeric flavoenzyme glutathione reductase from human erythrocytes has been elucidated by an X-ray diffraction analysis at 0.3 nm resolution. The polypeptide chain has been traced, and the binding positions of FAD, NADP and glutathione have been determined. A mechanism for the electron transfer is discussed.