Lens lipids and maximum lifespan.

Chlorophenols comprise a major class of environmental contaminants. They are extensively used as insecticides, fungicides, mold inhibitors, antiseptics and disinfectants. We found some of these compounds to be strong inhibitors of crystallin. This oxidoreductase enzyme was isolated from camel lens and its enzymatic activity was inhibited by the chlorophenols tested in a time-independent but concentration-dependent manner. 2,4,5-Trichlorophenol was the most potent inhibitor (IC50 = 3μM; Ki=3.2μM) whereas 4-chlorophenol was the least potent (IC50 = 4.1 mM). There appeared to be a relationship between the degree of chlorination of the phenols and inhibition of crystallin activity. The position of the chlorine substituent on the phenol may also influence the potency of these compounds.

https://www.tandfonline.com/doi/pdf/10.3109/14756369809028343

Inhibition of camel lens zeta-crystallin/NADPH: quinone oxidoreductase activity by chlorophenols.

Camel lens zeta-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 microM. 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 microM for both NADPH and PQ. Examination of other benzoquinones suggested that the presence of -OH and -Cl on benzoquinone was essential for the inhibition.

https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/15216549700201431

Riskuwa A. Shehu

Papers

Inhibition of camel lens zeta-crystallin/NADPH: quinone oxidoreductase activity by chlorophenols.

Inhibition of camel lens ζ‐crystallin/NADPH:Quinone oxidoreductase activity by chloranilic acid