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- W2068230596 abstract "Dansyl chloride, at low molar ratio, inactivates ferredoxin-NADP reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.7.1). The complete protection afforded either by NADP or NADPH suggests a direct involvement of the active site. Experiments with [Me-14C]dansyl chloride showed that about 1.5 residues per flavin were dansylated: by differential labelling experiments using NADP, it has been proved that enzyme inactivation is due to dansylation of one residue. The group modified has been identified as the ϵ-amino group of a lysine. The pH-inactivation profile indicates that this essential group has an apparent pKa of 8.7. The dansylated flavoprotein seems to maintain its native conformation; it shows a fluorescent chromophore with a peak at 335 nm. The modified enzyme has lost the capacity to form a complex with NADP, nevertheless it interacts normally with ferredoxin. It is concluded that the loss of catalytic activity which parallels the dansylation of a lysyl residue occurs because this residue is essential for the binding of the pyridine nucleotide substrate. Protection experiments with a series of coenzyme analogs further indicate that this lysyl residue interacts, most likely, with the 2′-phosphate moiety of NADP(H)." @default.
- W2068230596 created "2016-06-24" @default.
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- W2068230596 date "1976-08-01" @default.
- W2068230596 modified "2023-09-25" @default.
- W2068230596 title "A lysyl residue at the NADP binding site of ferredoxin-NADP reductase" @default.
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- W2068230596 doi "https://doi.org/10.1016/0005-2744(76)90157-1" @default.
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