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  • Title: Arginyl residues of adrenodoxin reductase as the anion recognition site for 2'-phosphate group of NADP+1.
    Author: Nonaka Y, Sugiyama T, Yamano T.
    Journal: J Biochem; 1982 Dec; 92(6):1693-701. PubMed ID: 7161255.
    Abstract:
    Adrenodoxin reductase from bovine adrenocortex was inactivated by arginine specific reagents, p-hydroxyphenylglyoxal, phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione. Inactivation of the enzyme caused by p-hydroxyphenylglyoxal obeyed pseudo-first-order kinetics and resulted in complete elimination of NADPH-ferricyanide reductase activity. The rate of inactivation increased with pH from 6.5 to 9.5. Ten out of 30-33 arginyl residues of the enzyme were modified, but residues essential to its enzymatic activity were less than 5. NADP+ strongly protected against inactivation by p-hydroxyphenylglyoxal, whereas NAD+ could afford only partial, weak protection. Furthermore, 2'-AMP and 2',5'-ADP afforded considerable protection but 5'-AMP did not. These data suggest that adrenodoxin reductase has essential arginyl residues which are crucial to the enzymatic activity as the recognition site for the negatively charged 2'-phosphate group of NADP+.
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