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Free keywords:
Glutathione Reductase; Riboflavin Deficiency; Mercuric Reductase; Lipoamide Dehydrogenase; Chain Fold
Abstract:
About 50 years ago FMN (Theorell 1935) and FAD (Warburg and Christian 1938) were discovered as prosthetic groups of the old yellow enzyme and of D-amino acid oxidase, respectively. More than 100 flavoenzymes have been described in the meantime (Dixon and Webb 1979); for four of them, structural data are known. These are glycolate oxidase (Lind quist and Bränden 1980), an FMN-dependent enzyme which probably has a chain fold in common with triose phosphate isomerase and one domain of pyruvate kinase, and three FAD-dependent enzymes: ferredoxin-NADP+ reductase (Sheriff and Herriott 1981; Karplus and Herriott 1982) p-hydroxybenzoate hydroxylase (Wierenga et al. 1979; Wierenga et al. 1982; Weijer et al. 1982) and glutathione reductase (Schulz et al. 1978; Thieme et al. 1981; Pai and Schulz 1983). The last mentioned two enzymes have been analyzed in atomic detail. In our presentation, we shall first describe glutathione reductase as a we11-understood flavoenzyme and then compare its structure with p-hydroxybenzoate hydroxylase. Whenever possible we shall include structural aspects of other flavoproteins in our discussion.
