PubMed · 9935312
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S P East. 1998. Combing the web.. https://doi.org/10.1016/s1074-5521(98)90669-x
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Last week, the giant publishing house Elsevier Science launched the first electronic archive for chemistry preprints through its ChemWeb subsidiary. The new site (preprint.chemweb.com) will be a common repository for reports on a wide range of chemistry topics and a forum for authors and readers to discuss the results. But ChemWeb could face an uphill battle in convincing authors to post their papers on the site, as many of the field's premier journals decline to accept papers that have already been posted on the Web.
[reaction: see text]A shape-persistent cyclic array of six zinc porphyrins provides an effective host for a dipyridyl-substituted free base porphyrin, yielding a self-assembled structure for studies of light harvesting. Energy transfer occurs essentially quantitatively from uncoordinated to pyridyl-coordinated zinc porphyrins in the cyclic array. Energy transfer from the coordinated zinc porphyrin to the guest free base porphyrin is less efficient (phitrans approximately 40%) and is attributed to a Förster through-space process.
Organophosphorus pesticides are the most common classes involved in poisonings related to pesticides. We used enzymatic activity of chloroperoxidase on the metabolism of some phosphorothioate pesticides published previously and molecular mechanics methods to perform a theoretical approach of the mechanism of biological oxidation of this class of pesticides. The molecular structure of eight pesticides were optimized by molecular mechanics methods using the CAChe program package for biomolecules, ver. 3.11 (Oxford Molecular Ltd., Campbell, CA). Total energy resulted from the structure optimization process and the partial charges of both phosphorus and sulfur were computed for every pesticide. Phosphorus partial charge and enzymatic activity were significantly related by linear regression analysis (r=0.82, P<0.05). Analyzing our results and using previously reported enzymatic activity of chloroperoxidase on these pesticides, we deduced chemical events involved in activation of the active site of chloroperoxidase and proposed a novel mechanism of oxidation for this class of pesticides. This mechanism will also help to understand the oxidation process of pesticides by cytochrome P450, and production of toxic metabolites.