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Inhibition of camel lens ζ‐crystallin/NADPH:Quinone oxidoreductase activity by chloranilic acid
Author(s) -
AlHamidi Abdulaziz A. A.,
Shehu Riskuwa A.,
Duhaiman Ali S.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201431
Subject(s) - chloranilic acid , chemistry , oxidoreductase , benzoquinone , electron acceptor , quinone , stereochemistry , chemiluminescence , biochemistry , enzyme , organic chemistry , chromatography
Camel lens ζ‐crystallin/NADPH:quinone oxidoreductase activity was inhibited by chloranilic acid (2,5‐dichloro‐3,6‐dihydroxy‐1,4‐benzoquinone) with NADPH as an electron donor and 9,10‐phenanthrenequinone (PQ) as an electron acceptor in a time‐independent but concentration dependent manner. The IC50 of chloranilic acid was 1 μM. The inhibition was noncompetitive with respect to both NADPH and PQ as deduced by Lineweaver‐Burk plots. The estimated inhibition constant (Ki) was 0.8 μM for both NADPH and PQ. Examination of other benzoquinones suggested that the presence of ‐OH and ‐Cl on benzoquinone was essential for the inhibition.