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Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues

Year: 1991

Type: article

Abstract: FAD-modified human glutathione reductases were reconstituted from apoenzyme using the FAD analogues 6-SH-FAD, 6-SCN-FAD, 6-OH-FAD, 6-NH2-FAD and 8-OH-FAD. The catalytic activities of the modified enzymes were substantially lower than for the native enzyme. All five species could be crystallized, but only those containing 6-SH-FAD, 6-OH-FAD and 6-NH2-FAD yielded crystals that could be analyzed. X-ray analyses and structural refinements were performed at 0.27 nm and 0.30 nm resolution resulting in R factors around 13.5%. The crystal structures showed the additional non-hydrogen atoms and small conformational changes of the polypeptide that were obviously induced by the substituents of the FAD analogues. The observed changes together with spectroscopic and activity data permit some conclusions about the chemical nature of the substituents.

Source: European Journal of Biochemistry

DOI: 10.1111/j.1432-1033.1991.tb16100.x

Authors: Ulrich ERMLER, Sandro GHISLA, Vincent MASSEY, Georg E. SCHULZ

Institutions: University of Freiburg, University of Konstanz, University of Michigan

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funders: Deutsche Forschungsgemeinschaft, National Institute of General Medical Sciences

Award: G2869093499