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  • Title: The NADP+-binding site of ferredoxin-NADP+ reductase. Sequence of the peptide containing the essential lysine residue.
    Author: Cidaria D, Biondi PA, Zanetti G, Ronchi S.
    Journal: Eur J Biochem; 1985 Jan 15; 146(2):295-9. PubMed ID: 3917922.
    Abstract:
    The flavoprotein ferredoxin-NADP+ reductase is inactivated and loses its ability to bind NADP+ during covalent modification of a lysine by 5-dimethylaminonaphthalene-1-sulfonyl chloride (dansyl chloride) [Zanetti, G. (1976) Biochim. Biophys. Acta 445, 14-24]. The substrate NADP+ gives almost complete protection against inactivation and modification. These observations are extended in this report by the characterization of an octapeptide containing the dansyl-lysine which was isolated by high-performance liquid chromatography from tryptic digests of protein modified with radiolabeled reagent. The amount of this peptide was severely reduced in protein modified in the presence of NADP+. The sequence of the dansyl-peptide, only partially obtained by Edman degradation, was completed by analysis of the fragments resulting from thermolysin digestion of the purified tryptic dansyl-peptide. Thus, the octapeptide containing the essential lysine residue has the following sequence: H2N-Ser-Val-Ser-Leu-Cys-Val-Lys-Arg-COOH. A comparison with corresponding sequences of other known NADP+-dependent dehydrogenases is attempted.
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