Characterization of the active center of thioredoxin reductase.
作者： Giuliana Zanetti , Charles H. Williams
DOI: 10.1016/S0021-9258(18)99416-0
关键词: Stereochemistry 、 Thioredoxin reductase 、 Redox 、 Cysteic acid 、 Chemistry 、 Thioredoxin 、 Flavin group 、 Inorganic chemistry 、 Ferredoxin-thioredoxin reductase 、 Dithionite 、 Dithiol
摘要: Abstract Reduction of thioredoxin reductase with different reductants has been followed spectrally; by titration TPNH in the presence DPNase or dithionite, it shown that this enzyme can accept 4 electrons per FAD. Thus, an additional acceptor group is postulated and identified as a disulfide which undergoes reversible reduction to dithiol. The activity very sensitive low concentrations mercurial, whereas transhydrogenase requires much higher levels for inhibition. Prereduction enhances former, but not latter process. Amperometric titrations show cysteic acid residues FAD, determined amino analysis, arise from 2 free sulfhydryls bond reducible TPNH. Mercurials are shown, spectral experiments, shift flavin second redox trapping action on nascent dithiol; after such treatment, completely reduced only FAD cannot be reoxidized thioredoxin.
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